BIOCHEM MIDTERM REVIEWER (Section 20.11).

A nonpolar amino acid is an amino

acid that contains one amino group, one carboxyl
PROTEINS group, and a nonpolar side chain. When incorporated
into a protein, such amino acids are hydrophobic
- A protein is a naturally-occurring, unbranched (“water-fearing”); that is, they are not attracted to
polymer in which the monomer units are amino water molecules.
acids
- Elemental composition - Contain Carbon (C), They are generally found in the interior of proteins,
Hydrogen (H), Nitrogen (N), Oxygen (O), most where there is limited contact with water. There are
also contain Sulfur (S) nine nonpolar amino acids. Tryptophan is a borderline
- The average nitrogen content of proteins is 15.4% member of this group because water can weakly
by mass interact through hydrogen bonding with the NH ring
- Also present are Iron (Fe), phosphorus (P) and location on tryptophan’s side-chain ring structure.
some other metals in some specialized proteins Thus, some textbooks list tryptophan as a polar
neutral amino acid. The three types of polar amino
AMINO ACIDS acids have varying degrees of affi nity for water.
Within a protein, such amino acids are said to be
An organic compound that contains both an amino (- hydrophilic (“water-loving”). Hydrophilic amino acids
NH2) and carboxyl (-COOH) groups attached to same are often found on the surfaces of proteins.
carbon atom
A polar neutral amino acid is an amino acid that
The position of carbon atom is Alpha (a) contains one amino group, one carboxyl group, and a
-NH2 group is attached at alpha (a) carbon atom. side chain that is polar but neutral. In solution at
physiological pH, the side chain of a polar neutral
-COOH group is attached at alpha (a) carbon atom. amino acid is neither acidic nor basic. There are six
polar neutral amino acids. These amino acids are
R = side chain –vary in size, shape, charge, acidity, more soluble in water than the nonpolar amino acids
functional groups present, hydrogen-bonding ability, as, in each case, the R group present can hydrogen
and chemical reactivity. bond to water.

>700 amino acids are known A polar acidic amino acid is an amino acid that
contains one amino group and two carboxyl groups,
Based on common “R” groups, there are 20 standard the second carboxyl group being part of the side
amino acids chain. In solution at physiological pH, the side chain of
a polar acidic amino acid bears a negative charge; the
All amino acids differ from one another by their R- side-chain carboxyl group has lost its acidic hydrogen
groups atom. There are two polar acidic amino acids: aspartic
Standard amino acids are divided into four groups acid and glutamic acid.
based on the properties of R-groups A polar basic amino acid is an amino acid that
Non-polar amino acids: R-groups are non-polar contains two amino groups and one carboxyl group,
the second amino group being part of the side chain.
Such amino acids are hydrophobic-water fearing In solution at physiological pH, the side chain of a
(insoluble in water) polar basic amino acid bears a positive charge; the
nitrogen atom of the amino group has accepted a
8 of the 20 standard amino acids are non polar proton (basic behavior; Section 17.6). There are three
polar basic amino acids: lysine, arginine, and histidine.
When present in proteins, they are located in the
interior of protein where there is no polarity. NOMENCLATURE

A standard amino acid is one of the 20 a-amino acids Common names assigned to the amino acids are
normally found in proteins. The structures of the 20 currently used.
standard amino acids are given in Table 20.1. Within
Table 20.1, amino acids are grouped according to Three letter abbreviations - widely used for naming:
side-chain polarity. In this system there are four
categories: (1) nonpolar amino acids, (2) polar neutral First letter of amino acid name is compulsory and
amino acids, (3) polar acidic amino acids, and (4) capitalized followed by next two letters not capitalized
polar basic amino acids. This classifi cation system except in the case of Asparagine (Asn), Glutamine
gives insights into how various types of amino acid (Gln) and tryptophan (Trp).
side chains help determine the properties of proteins
 One-letter symbols - commonly used for comparing Isoelectric point (pI) – pH at which the concentration of
amino acid sequences of proteins: Zwitterion is maximum -- net charge is zero

Usually the first letter of the name Different amino acids have different isoelectric points

When more than one amino acid has the same letter At isoelectric point - amino acids are not attracted towards
the most abundant amino acid gets the 1st letter an applied electric field because they net zero charge.

CHIRALITY AND AMINO ACIDS CYSTEINE: A CHEMICALY UNIQUE AMINO ACID

Four different groups are attached to the a-carbon the only standard amino acid with a sulfhydryl group ( —
atom in all of the standard amino acids except glycine SH group).

In glycine R-group is hydrogen The sulfhydryl group imparts cysteine a chemical property
unique among the standard amino acids.
Therefore 19 of the 20 standard amino acids contain a
chiral center Cysteine in the presence of mild oxidizing agents
dimerizes to form a cystine molecule.
Chiral centers exhibit enantiomerism (left- and right-
handed forms) Cystine - two cysteine residues linked via a covalent
disulfide bond.
Each of the 19 amino acids exist in left and right
handed forms PEPTIDES

The amino acids found in nature as well as in proteins Dipeptide: bond between two amino acids
are L isomers.
Oligopeptide: bond between ~ 10 - 20 amino acids
Bacteria do have some D-amino acids
Polypeptide: bond between large number of amino acids
With monosaccharides nature favors D-isomers
Every peptide has an N-terminal end and a C-terminal end
The rules for drawing Fischer projection formulas for
+
amino acid structures H3N-aa-aa-aa-aa-aa-aa-aa-aa-aa-COO-

The — COOH group is put at the top, the R group at PEPTIDE NOMENCLATURE
the bottom to position the carbon chain vertically
RULE 1. The C-terminal amino acid residue keeps its full
The — NH2 group is in a horizontal position. amino acid name.

Positioning — NH2 on the left - L isomer RULE 2. All of the other amino acid residues have names
that end in -yl. The -yl suffi x replaces the -ine or -ic acid
Positioning — NH2 on the right - D isomer. ending of the amino acid name, except for tryptophan, for
which -yl is added to the name.
ACID BASE PROPERTIES OF AMINO ACIDS
RULE 3. The amino acid naming sequence begins at the
In pure form amino acids are white crystalline solids N-terminal amino acid residue.
Most amino acids decompose before they melt Example:
Not very soluble in water Ala-leu-gly has the IUPAC name of alanylleucylglycine
Exists as Zwitterion: An ion with + (positive) and – ISOMERIC PEPTIDES
(Nagetive) charges on the same molecule with a net
zero charge Peptides that contain the same amino acids but present in
different order are different molecules (constitutional
Carboxyl groups give-up a proton to get negative charge isomers) with different properties
Amino groups accept a proton to become positive For example, two different dipeptides can be formed
between alanine and glycine
Amino acids in solution exist in three different species
(zwitterions, positive ion, and negative ion) - Equilibrium The number of isomeric peptides possible increases
shifts with change in pH rapidly as the length of the peptide chain increases
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES Several proteins with >10,000 amino acid residues are
known
Many relatively small peptides are biochemically active:
Common proteins contain 400–500 amino acid residues
Hormones
Small proteins contain 40–100 amino acid residues
Neurotransmitters
More than one peptide chain may be present in a protein:
Antioxidants
Monomeric : A monomeric protein contains one peptide
Small Peptide Hormones: chain
Best-known peptide hormones: oxytocin and vasopressin Multimeric: A multimeric protein contains more than one
peptide chain
Produced by the hypothalamus stored in the posterior
pituitary gland PROTEIN CLASSSIFICATION BASED ON CHEMICAL
COMPOSITION
nonapeptide (nine amino acid residues) with six of the
residues held in the form of a loop by a disulfide bond Simple proteins: A protein in which only amino acid
formed between two cysteine residues residues are present:
SMALL PEPTIDE NEUROTRANSMITTERS More than one protein subunit may be present but all
subunits contain only amino acids
Enkephalins are pentapeptide neurotransmitters produced
by the brain and bind receptor within the brain Conjugated protein: A protein that has one or more non-
amino acid entities (prosthetic groups) present in its
Help reduce pain structure:
Best-known enkephalins: One or more polypeptide chains may be present
Met-enkephalin: Tyr–Gly–Gly–Phe–Met Non-amino acid components - may be organic or inorganic
Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu - prosthetic groups

SMALL PEPTIDES ANTIOXIDANTS Lipoproteins contain lipid prosthetic groups

Glutathione (Glu–Cys–Gly) – a tripeptide – is present is in Glycoproteins contain carbohydrate groups,

high levels in most cells Metalloproteins contain a specific metal as prosthetic
Regulator of oxidation–reduction reactions. group

Glutathione is an antioxidant and protects cellular contents FOUR TYPES OF STRUCTURES

from oxidizing agents such as peroxides and superoxides PRIMARY STRUCTURE

Highly reactive forms of oxygen often generated within the Primary structure of protein refers to the order in which
cell in response to bacterial invasion amino acids are linked together in a protein
Unusual structural feature – Glu is bonded to Cys through Every protein has its own unique amino acid sequence
the side-chain carboxyl group.
Frederick Sanger (1953) sequenced and determined the
GENERAL STRUCTURAL CHARACTERISTICS OF primary structure for the first protein - Insulin
PROTEINS

A protein is a naturally-occurring, unbranched polymer in

which the monomer units are amino acids. SECONDARY STRUCTURE
A protein is a peptide in which at least 40 amino acid Arrangement of atoms of backbone in space.
residues are present:
The two most common types : alpha-helix (a-helix) and the
The terms polypeptide and protein are often used beta-pleated sheet (b-pleated sheet).
interchangeably used to describe a protein
The peptide linkages are essentially planar thus allows Hydrophobic interactions: Between non-polar side chains
only two possible arrangements for the peptide backbone
for the following reasons: QUATERNANRY STRUCTURE

For two amino acids linked through a peptide bond six The HIGHEST level of protein organization
atoms lie in the same plane
Most multimeric proteins contain an even number of
The planar peptide linkage structure has considerable subunits (two subunits a dimer, four subunits a tetramer,
rigidity, therefore rotation of groups about the C–N bond is and so on).
hindered
The subunits are held together mainly by hydrophobic
Cis–trans isomerism is possible about C–N bond. interactions between amino acid R groups.

The trans isomer is the preferred orientation An example of a protein with quaternary structure is
hemoglobin, the oxygen carrying protein in blood. It is a
Alpha-helix (a-helix) tetramer in which there are two identical a chains and two
identical B chains. Each chain enfolds a heme group, the
A single protein chain adopts a shape that resembles a site where oxygen binds to the protein.
coiled spring (helix):
PROTEIN CLASSIFICATION BASED ON SHAPE
H-bonding between same amino acid chains –intra
molecular Most abundant proteins in humans (30% of total body
protein)
Coiled helical spring
Major structural material in tendons, ligaments, blood
R-group outside of the helix -- not enough room for them to vessels, and skin
stay inside
Organic component of bones and teeth
Beta-pleated sheets
Predominant structure - triple helix
Completely extended amino acid chains
Rich in proline (up to 20%) – important to maintain
H-bonding between two different chains – inter and/or structure
intramolecular
PROTEIN CLASSIFICATION BASED ON SHAPE
Side chains below or above the axis
Myoglobin:

An oxygen storage molecule in muscles.

TERTIARY STRUCTURE
Monomer - single peptide chain with one heme unit
The overall three-dimensional shape of a protein
Binds one O2 molecule
Results from the interactions between amino acid side
chains (R groups) that are widely separated from each Has a higher affinity for oxygen than hemoglobin.
other.
Oxygen stored in myoglobin molecules serves as a reserve
In general 4 types of interactions are observed. oxygen source for working muscles

FOUR TYPES OF INTERACTIONS Hemoglobin:

Disulfide bond: covalent, strong, between two cysteine An oxygen carrier molecule in blood
groups
Transports oxygen from lungs to tissues
Electrostatic interactions: Salt Bridge between charged
side chains of acidic and basic amino acids Tetramer (four peptide chains) - each subunit has a heme
group
-OH, -NH2, -COOH, -CONH2
Can transport up to 4 oxygen molecules at time
H-Bonding between polar, acidic and/or basic R groups
Iron atom in heme interacts with oxygen
For H-bonding to occur, the H must be attached on O, N or
F
MAJOR CATEGORIES OF PROTEINS BASED ON Nutrient proteins: Particularly important in the early
FUNCTION stages of life - from embryo to infant.

Catalytic proteins: Enzymes are best known for their Casein (milk) and ovalalbumin (egg white) are nutrient
catalytic role. proteins

Almost every chemical reaction in the body is driven by an Milk also provide immunological protection for mammalian
enzyme young.

Defense proteins: Immunoglobulins or antibodies are PROTEIN HYDROLYSIS

central to functioning of the body’s immune system.
Results in the generation of an amine and a carboxylic acid
Transport proteins: Bind small biomolecules, e.g., oxygen functional groups.
and other ligands, and transport them to other locations in
the body and release them on demand. Digestion of ingested protein is enzyme-catalyzed
hydrolysis
Messenger proteins: transmit signals to coordinate
biochemical processes between different cells, tissues, Free amino acids produced are absorbed into the
and organs. bloodstream and transported to the liver for the synthesis
of new proteins.
Insulin and glucagon - regulate carbohydrate metabolism
Hydrolysis of cellular proteins and their resynthesis is a
Human growth hormone – regulate body growth continuous process.

Contractile proteins: Necessary for all forms of PROTEIN DENATURATION

movement.
Partial or complete disorganization of protein’s tertiary
Muscles contain filament-like contractile proteins (actin and structure
myosin).
Cooking food denatures the protein but does not change
Human reproduction depends on the movement of sperm protein nutritional value
– possible because of contractile proteins.
Coagulation: Precipitation (denaturation of proteins)
Structural proteins: Confer stiffness and rigidity
Egg white - a concentrated solution of protein albumin -
Collagen is a component of cartilage a forms a jelly when heated because the albumin is
denatured
Keratin gives mechanical strength as well as protective
covering to hair, fingernails, feathers, hooves, etc. Cooking:

Transmembrane proteins: Span a cell membrane and Denatures proteins – Makes it easy for enzymes in our
help control the movement of small molecules and ions. body to hydrolyze/digest protein

Have channels – help molecules can enter and exit the Kills microorganisms by denaturation of proteins
cell.
Fever: >104ºF – the critical enzymes of the body start
Transport is very selective - allow passage of one type of getting denatured
molecule or ion.
GLYCOPROTEINS
Storage proteins: Bind (and store) small molecules.
Conjugated proteins with carbohydrates linked to
Ferritin - an iron-storage protein - saves iron for use in the them:
biosynthesis of new hemoglobin molecules.
Many of plasma membrane proteins are glycoproteins
Myoglobin - an oxygen-storage protein present in muscle
Blood group markers of the ABO system are also
Regulatory proteins: Often found “embedded” in the glycoproteins
exterior surface of cell membranes - act as sites for
receptor molecules Collagen and mmunoglobulins are glycoproteins

Often the molecules that bind to enzymes (catalytic Collagen -- glycoprotein

proteins), thereby turning them “on” and “off,” and thus
controlling enzymatic action.
 Most abundant protein in human body (30% of total body Five Categories of Lipids
protein)
• For purposes of simplicity of study lipids are divided
Triple helix structure into five categories based on their function:

Rich in 4-hydroxyproline (5%) and 5-hydroxylysine (1%) — – Energy-storage lipids - triacylglycerols

derivatives
– Membrane lipids - phospholipids,
Some hydroxylysines are linked to glucose, galactose, and sphingoglycolipids, and cholesterol
their disaccharides – help in aggregation of collagen fibrils.
-Emulsification lipids - bile acids
Immunoglobulins
-Chemical messenger lipids - steroid hormones and
Glycoproteins produced as a protective response to the eicosanoids)
invasion of microorganisms or foreign molecules -
antibodies against antigens. -Protective-coating lipids - biological waxes

Immunoglobulin bonding to an antigen via variable region Structural Formulas

of an immunoglobulin occurs through hydrophobic
interactions, dipole – dipole interactions, and hydrogen • Lipids exhibit structural diversity
bonds. • Some are esters, some are amides, and some are
LIPOPROTEINS alcohols (acyclic and cyclic) and some are
polycyclic.
a conjugated protein that contains lipids in addition to
amino acids Saturated and Unsaturated Fatty Acids

help suspend lipids and transport them through the • Carboxylic acids with linear (unbranched) carbon
bloodstream chain - Fatty acids are naturally occuring
monocarboxylic acids
Four major classes of plasma lipoproteins:
• Even # of Carbon atoms:
Chylomicrons: Transport dietary triacylglycerols from
intestine to liver and to adipose tissue. – Long chain fatty acids: C12 - C26

Very-low-density lipoproteins (VLDL): Transport – Medium chain fatty acids: C6 - C11

triacylglycerols synthesized in the liver to adipose tissue. – Short-chain fatty acids: C4 - C5
Low-density lipoproteins (LDL): Transport cholesterol • Two Types:
synthesized in the liver to cells throughout the body.
– Saturated - all C-C bonds are single bonds
High-density lipoproteins (HDL): Collect excess
cholesterol from body tissues and transport it back to the – Unsaturated
liver for degradation to bile acids.
– Monounsaturated: one C=C bond
Lipids
– Polyunsaturated: 2 or more C=C bonds
• A lipid is an organic compound found in living present - up to six double bonds are present
organisms that is insoluble (or only sparingly in fatty acids
soluble) in water but soluble in non-polar organic
solvents. Saturated Fatty Acids

• Unlike other biomolecules, lipids do not have a – Numbering starts from the end of -COOH group
common structural features that serves as the basis
for defining such compounds. – See structural notation: it indicates number of C
atoms
• Classification: They are classified on the basis of
solubility not on any functional groups – Example - Lauric acid has 12 C atoms and no
double bonds so it is (12:0)
– Insoluble or sparingly soluble in water
Unsaturated Fatty Acids
– Soluble in non-polar organic solvents
 • A monounsaturated fatty acid is a fatty acid with a • Deficient in omega 3 fatty acids
carbon chain in which one carbon–carbon double
bond is present. – Fish - good source for omega 3 fatty acids

• Different ways of depicting the structure • High rate of heart disease may be due to imbalance
in omega 3 and 6 fatty acids
Polyunsaturated Fatty Acids (PUFAs)
– Ideal ratio: Omega 6 : Omega 3 (4 - 10 g:
• A polyunsaturated fatty acid is a fatty acid with a 1g)
carbon chain in which two or more carbon–carbon
double bonds are present. • Water solubility: Short chain fatty acids have some
solubility whereas long chain fatty acids are
• Up to six double bonds are found in biochemically insoluble
important PUFAs.
– Short chain fatty acids are sparingly soluble
• Two types of unsaturated fatty acids. because of carboxylic acid polar group

– Omega (ω)-3 fatty acids - An unsaturated • Physical properties such as melting point depends
fatty acid with its endmost double bond on the number of C atoms and degree unsaturation
three carbon atoms away from its methyl
end. The Melting Point

– Omega(ω)-6 fatty acid is an unsaturated • Melting Point Depends Upon:

fatty acid with its endmost double bond six
carbon atoms away from its methyl end. – Length of carbon chain

Selected Unsaturated Fatty Acids of Biological – Degree of unsaturation (number of double

Importance bonds in a molecule)

• Numbering starts from the other end of COOH Space-Filling Molecules

• See structural notation: it indicates number of C • The number of bends in a fatty acid chain increase
atoms as the number of double bonds increase

• E.g., 18:2 – 18 carbons, 2 double bonds • Less packing occurs

Omega Acids • Melting point is lower

• Essential Fatty Acids: Must be part of diet • Tend to be liquids at room temperature

• Nutritionally important Omega-3 and Omega-6 fatty

acids Energy-Storage Materials
– Linolenic acid – Omega-3 • With the notable exception of nerve cells, human
– Linoleic acid – Omega-6 cells store small amounts of energy providing
materials:
• Linoleic Acid Deficiency:
– The most widespread energy storage
– Skin redness - becomes irritated material -carbohydrate glycogen

– Infections and dehydration – Present in small amounts

– Liver abnormalities • Storage material is the triacylglycerols:

– Children need it the most – Triacylglycerols are concentrated primarily

in special cells (adipocytes)
– Human milk has more than cow’s milk
– Nearly filled with the material.
American Diet
Two Types of Triacylglycerols
• Sufficient in omega 6 fatty acids
 • Simple Triacylglycerols: Three identical fatty acids – Current recommended amounts are: total
are esterified fat intake in calories:

– Naturally occurring simple triacylglycerols • 15% - Monounsaturated fat

are rare
• 10% - Polyunsaturated
• Mixed Triacylglycerols: A triester formed from the
esterification of glycerol with more than one kind of • <10% - Saturated fats
fatty acid
• Studies also indicate that:
– In nature mostly mixed triacylglycerols are
found and are different even from the same – Saturated fats are considered “bad fats”
source depending on the feed, e.g., corn, – Monounsaturated fats are considered “good
peanut and wheat -fed cows have different fats”
triacylglycerols
– Trans-monounsaturated fats are considered
Difference of Fats and Oils “bad fats”
• Physical State: – Polyunsaturated fats can be both “good
– Fats fats” and “bad fats”

• Predominantly Saturated • Omega 3 and 6 are important “good

fats”
• Solids or semisolids at room
temperature Essential Fatty Acids

– Oils: • Fatty acids that must be obtained from dietary

sources – are not synthesized within the body
• Predominantly unsaturated
• Two most important essential fatty acids are:
• Liquids at room temperature
– Linoleic acid (18:2) - omega 6
• Source:
– Linolenic acid (18:3) - omega 3
– Fats: Animal source and tasteless
• Both are needed for:
– Oils: Plants and fish oil
– Proper membrane structure
– Pure oils and fats are colorless, odorless
– Serve as starting materials
Studies for the production of several
nutritionally important longer-
• Nations whose citizens have high dietary intakes of chain omega-6 and omega-3
fats and oils tend to have higher incidences of heart fatty acids
disease and certain types of cancers
• Deficiencies of above two acids may result in skin
• Typical American diet contains too much fat and redness, infections and dehydration likely and liver
therefore the Americans are being asked to reduce abnormalities may develop
their total dietary fat intake
Fat and Fatty Acid Composition of Nuts
• Other studies show that risk factor is more than
simply the total amount of triacylglycerols • Numerous studies now indicate that eating nuts can
consumed have a strong protective effect against coronary
heart disease:

– Low amounts of saturated fatty acids

“Good Fats” Versus “Bad Fats”
– Nuts also contain valuable antioxidant
• Studies indicate that type of dietary fat and amount vitamins, minerals, and plant fiber protein
of dietary fat are important for balanced diet:
Partial Hydrolysis
 • Chemical Properties due to two functional groups: • Triacylglycerols serve as energy storage
esters and alkenes molecules

– Hydrolysis: Partial hydrolysis of • Glycerophospholipids function as

triacylglycerols components of cell membranes

– Breaking of 1-2 ester bonds to give rise to • A major structural difference between the two types
mono- or diacylglycerol and fatty acid(s) of lipids is that of their “polarity” – Responsible for
the their differing biochemical functions.
– Carried out by enzymes produced by the
pancreas • Triacylglycerols are a non-polar

Saponification • Glycerophospholipids are polar.

• Hydrolysis in basic solution: Produce salt of fatty Sphingophospholipids

acid and glycerol
• Structures based on the 18-carbon
RCOOR’ + NaOH  RCOONa (soap) + monounsaturated aminodialcohol sphingosine
R’OH
• contains one fatty acid and one phosphate group
Hydrogenation attached to a sphingosine molecule and an alcohol
attached to the phosphate group
– Addition of hydrogen across double (=)
bond - increases degree of saturation • Saponifiable lipids

– Many food products are produced by partial • Sphingophospholipids in which the alcohol
hydrogenation of oils and fats esterified to the phosphate group is choline are
called sphingomyelins.
– Peanut oil + H2  Peanut Butter
• Sphingomyelins are found in all cell membranes
– Vegetable oil + H2  Margerine and are important structural components of the
myelin sheath of neurons
Glycerophospholipids
• Sphingoglycolipids: Contains both a fatty acid and
• A glycerophospholipid is a lipid that contains two carbohydrate
fatty acids and a phosphate group esterified to a
glycerol molecule and an alcohol esterified to the • Simple sphingoglycolipids are called cerebrosides:
phosphate group. contains a single monosaccharide unit - either
glucose or galactose
• All attachments (bonds) between groups in a
glycerophospholipid are ester linkages They occur primarily in brain (7% of dry mass)
• Glycerophospholipids have four ester linkages as Gangliosides
contrasted to three ester linkages in
triacylglycerols. • Complex sphingoglycolipids are called
Gangliosides: contain a branched chain of up to
• Glycerophospholipids undergo hydrolysis and seven monosaccharide residues.
saponification reactions in a manner similar to that
for triacylglycerols • Occur in the gray matter of the brain as well as in
the myelin sheath.
• The alcohol attached to the phosphate group in a
glycophospholipid is usually one of three amino Cholesterol-Third major type of membrane lipid
alcohols: choline, ethanolamine, or serine -
respectively known as phosphatidylcholines, • Lipids: Fused Rings
phosphatidylethanolamines, and
phosphatidylserines. • Cholesterol: C27 steroid molecule

• Structurally glycerophospholipids are alghough • A steroid is a lipid whose structure is based on a

similar to triacylglycerols, they have different fused ring system of three 6 carbon rings and one 5
biochemical functions. carbon ring.

• Important in human cell membranes, nerve tissue

and brain tissue
 – Important in chemical synthesis: Hormones, – Receptors for hormones and
vitamins essential for life neurotransmitters

Cholesterol in Food • The membrane proteins and some lipids are further
reacted with carbohydrates molecules:
• Liver synthesizes cholesterol: ~ 1g everyday; so it
is not necessary to consume in the form of diet – Act as markers: process by which different
cells recognize each other
• Cholesterol synthesis decrease if it is ingested but
reduction is not sufficient: Leads to cardiovascular Passive Transport
disease
• Transport Across Cell Membranes:
• Animal Food: Lot of cholesterol
– To maintain cellular processes various
• Plant Food: No cholesterol molecules transported across the cell
membranes.
Cells
– Three types of transport.
• Cells are surrounded by plasma membranes:
• Passive transport
– Separates aqueous interior of a cell from
the aqueous environment surrounding the • Facilitated transport
cell
• Active transport
– Up to 80% of plasma membrane is lipid
material • Passive transport - a substance moves across a
cell membrane by diffusion from a region of higher
– The membranes are lipid bilayer made up of concentration to a region of lower concentration.
phospholipids
– Only a few types of molecules, including O2,
• Cells are surrounded by plasma membranes: N2, H2O, urea, and ethanol, can cross
membranes by passive transport
- Bilayer: Nonpolar tails of phospholipids in the
middle and polar heads are on the surface Facilitated Transport

• 6 - 9 billionths of a meter thick or 6-9 • Facilitated transport - a substance moves across a

nanometer thick cell membrane with the aid of a membrane protein
from a region of higher concentration to a region of
- The membrane is a liquid like structure due to lower concentration.
unsaturation in lipid tails
– The specific protein carriers or transporters
Cholesterol are involved in the process
• Cholesterol molecules are also components of Active Transport
plasma membranes:
• Active transport - a substance moves across a cell
– Cholesterol helps regulate membrane membrane, with the aid of membrane proteins,
fluidity – The fused ring system does nor against a concentration gradient with the
allow rotation of fatty acid tails in the vicinity expenditure of cellular energy.
– Fits between fatty acid chains of the lipid – Proteins involved in active transport are
bilayer: Make it rigid called “pumps.” The needed energy is
supplied by molecules such as ATP.
– Cholesterol thus acts a membrane
plasticizer Emulsification lipids
Proteins • An emulsifier is a substance that can disperse and
stabilize water-insoluble substances as colloidal
• The membranes also contain proteins: particles in an aqueous solution.
– Responsible for moving substances such as
nutrients and electrolytes across the
membrane
 • Bile Acids: Cholesterol derivatives that functions as Adrenocorticoid Hormones
emulsifying agents that make dietary lipids soluble
in aqueous environment of the digestive tract: • Produced by the adrenal glands - small organs
located on top of each kidney
– Approximately one third of cholesterol
produced by liver is converted to bile acids. • 28 Different hormones have been isolated from the
adrenal cortex
– Action similar to soap in washing
• Two types of adrenocorticoid hormones:
Bile Acids
– Mineralocorticoids - control the balance of
• Bile acids are tri- or dihydroxy cholesterol Na and K ions in cells
derivatives
– Glucocorticoids - control glucose
• The carbon 17 side chain of cholesterol has been metabolism and counteract inflammation
oxidized to a carboxylic acid
• Eicosanoids Arachidonic acid (20:4) derivatives:
• The oxidized acid side chain is bonded to an amino
acid (either glycine or taurine) through an amide – Have profound physiological effects at
linkage extremely low concentrations.

• Bile is a fluid containing emulsifying agents (Bile – Eicosanoids are hormone-like molecules
acids) secreted by the liver, stored in the
gallbladder, and released into the small intestine – Exert their effects in the tissues where they
during digestion are synthesized.

Hormones – Eicosanoids usually have a very short “life.”

• A hormone is a biochemical substance produced by – Physiological effects of eicosanoids:

a ductless gland that has a messenger function. • Inflammatory response
• Hormones serve as a means of communication • Production of pain and fever
between various tissues.
• Regulation of blood pressure
– Some hormones are lipids.
• Induction of blood clotting
• The lipids that play the role of “chemical
messengers” include: • Control of reproductive functions, such as induction
of labor
– Steroid hormones – derivatives of
cholesterol • Regulation of the sleep/wake cycle
– Eicosanoids- derivatives of arachidonic acid Three Principle Types

• There are two major classes of steroid hormones: 1. Prostoglandins: C20-fatty-acid derivative containing
cyclopentane ring and oxygen-containing functional
– Sex hormones - control reproduction and groups
secondary sex characteristics
– Involved in raising body temperature,
– Adrenocorticoid hormones – control
numerous biochemical processes in the – Inhibiting the secretion of gastric juices,
body
– Increasing the secretion of a protective
Sex Hormones mucus layer into the stomach,
• Classified into three major groups: – Relaxing and contracting smooth muscle,
directing water and electrolyte balance,
– Estrogens - the female sex hormones intensifying pain, and enhancing
– Androgens - the male sex hormones inflammation responses.

– Progestins - the pregnancy hormones

 2. Thromboxanes: C20-fatty-acid derivative containing A nucleic acid is a polymer in which the monomer units
a cyclic ether ring and oxygen-containing functional are nucleotides.
groups
Two Types of Nucleic Acids:
Promote platelet aggregation.
DNA: Deoxyribonucleic Acid: Found within cell nucleus
3. Leukotrienes: C20-fatty-acid derivative containing
three conjugated double bonds and hydroxy groups Storage and transfer of genetic information

Promote inflammatory and hypersensitivity (allergy) Passed from one cell to other during cell division
responses
RNA: Ribonucleic Acid: Occurs in all parts of cell
• A biological wax: a monoester of a long-chain fatty
acid and a long-chain alcohol. Primary function is to synthesize the proteins

• The fatty acids found in biological waxes: NUCLEOTIDES

– Generally are saturated fatty acids Nucleic Acids: Polymers in which repeating unit is
nucleotide
– Contain 14 to 36 carbon atoms.
A Nucleotide has three components:
• The alcohols found in biological waxes:
Pentose Sugar: Monosaccharide
– May be saturated or unsaturated
Phosphate Group (PO43-)
– May contain 16 to 30 carbon atoms.
Heterocyclic Base
• Properties of Biological waxes : Water-insoluble
Pentose Sugar
and water-repellent because of long nonpolar
hydrocarbon chains. Ribose is present in RNA and 2-deoxyribose is present
in DNA
– Humans and animals secrete biological
waxes from skin glands Structural difference:
• Function of biological waxes: a —OH group present on carbon 2’ in ribose
– Protect hair and skin; and keep it pliable a —H atom in 2-deoxyribose
and lubricated.
RNA and DNA differ in the identity of the sugar unit in
– Impart water repellency to animal fur. their nucleotides.
– Birds keep their feathers water repellent and Phosphates
help minimize loss of body heat
Phosphate - is derived from phosphoric acid (H3PO4)
– Plants coat their leaves with a thin layer of
biological waxes to prevent excessive Under cellular pH conditions, the phosphoric acid is
evaporation of water and to protect against fully dissociated to give a hydrogen phosphate ion
parasite attack. (HPO42-)
• Nucleic Acids- are biopolymers made up of Nitrogen-Containing Heterocyclic Bases
monomeric units of NUCLEOTIDES
There are a total five bases (four of them in most of
Two important functions: DNA and RNAs)
• To hold genetic information Three pyrimidine derivatives - thymine (T), cytosine
(C), and uracil (U)
• To perform variety of other functions
Two purine derivatives - adenine (A) and guanine (G)
TYPES OF NUCLEIC ACIDS
Adenine (A), guanine (G), and cytosine (C) are found in
Nucleic Acids are found in nucleus and are acidic in both DNA and RNA.
nature
Uracil (U): found only in RNA
 Thymine (T) found only in DNA. Example: Human DNA contains 30% adenine, 30%
thymine, 20% guanine and 20% cytocine
NUCLEOTIDE FORMATION
DNA Sequence: the sequence of bases on one
The formation of a nucleotide from sugar, base, and polynucleotide is complementary to the other
phosphate is visualized below. polynucleotide
Phosphate attached to C-5’ and base is attached to C-1’ Complementary bases are pairs of bases in a nucleic acid
position of pentose structure that can hydrogen-bond to each other.

Complementary DNA strands are strands of DNA in a

double helix with base pairing such that each base is
located opposite its complementary base.

Example :

List of bases in sequential order in the direction from the 5’

end to 3’ end of the segment:

5’-A-A-G-C-T-A-G-C-T-T-A-C-T-3’

Complementary strand of this sequence will be:

PRIMARY NUCLEIC ACID STRUCTURE
3’-T-T-C-G-A-T-C-G-A-A-T-G-A-5’
Sugar-phosphate groups are referred to as nucleic acid
backbone - Found in all nucleic acids Base Pairing
Sugars are different in DNA and RNA One small and one large base can fit inside the DNA
strands:
PRIMARY STRUCTURE
Hydrogen bonding is stronger with A-T and G-C
A ribonucleic acid (RNA) is a nucleotide polymer in which
each of the monomers contains ribose, a phosphate group, A-T and G-C are called complementary bases
and one of the heterocyclic bases adenine, cytosine,
guanine, or uracil Replication: Process by which DNA molecules produce
exact duplicates of themselves
A deoxyribonucleic acid (DNA) is a nucleotide polymer in
which each of the monomers contains deoxyribose, a Old strands act as templates for the synthesis of new
phosphate group, and one of the heterocyclic bases strands
adenine, cytosine, guanine, or thymine.
DNA polymerase checks the correct base pairing and
Structure: Sequence of nucleotides in DNA or RNA catalyzes the formation of phosphodiester linkages

Primary structure is due to changes in the bases The newly synthesized DNA has one new DNA strand and
old DNA strand
Phosphodiester bond at 3’ and 5’ position
DNA polymerase enzyme can only function in the 5’-to-3’
5’ end has free phosphate and 3’ end has a free OH group direction

Sequence of bases read from 5’ to 3’ Therefore one strand (top; leading strand ) grows
continuously in the direction of unwinding
The DNA Double Helix
The lagging strand grows in segments (Okazaki fragments)
The secondary structure involves two polynucleotide
in the opposite direction
chains coiled around each other in a helical fashion
The segments are latter connected by DNA ligase
The poly nucleotides run anti-parallel (opposite directions)
to each other, i.e., 5’ - 3’ and 3’ - 5’ DNA replication usually occurs at multiple sites within a
molecule (origin of replication)
The bases are located at the center and hydrogen bonded
(A=T and GΞC) DNA replication is bidirectional from these sites (replication
forks)
Base composition: %A = %T and %C = %G)
Multiple-site replication enables rapid DNA synthesis Small nuclear RNA: Facilitates the conversion of hnRNA
to mRNA.
Upon DNA replication the large DNA molecules interacts
with histone proteins to fold long DNA molecules. Contains from 100 to 200 nucleotides

The histone–DNA complexes are called chromosomes: Ribosomal RNA (rRNA): Combines with specific proteins
to form ribosomes - the physical site for protein synthesis
A chromosome is about 15% by mass DNA and 85% by
mass protein. Ribosomes have molecular masses on the order of 3
million
Cells of different kinds of organisms have different
numbers of chromosomes. Transfer RNA (tRNA): Delivers amino acids to the sites
for protein synthesis
Example: Number of chromosomes in a human cell 46, a
mosquito 6, a frog 26, a dog 78, and a turkey 82 tRNAs are the smallest (75–90 nucleotide units)

Chromosomes occur in matched (homologous) pairs. Transcription: RNA Synthesis

Example: The 46 chromosomes of a human cell constitute Transcription: A process by which DNA directs the
23 homologous pairs synthesis of mRNA molecules

Overview of Protein Synthesis Two-step process - (1) synthesis of hnRNA and (2) editing
to yield mRNA molecule
Protein synthesis is directly under the direction of DNA
Gene: A segment of a DNA base sequence responsible for
Proteins are responsible for the formation of skin, hair, the production of a specific hnRNA/mRNA molecule
enzymes, hormones, and so on
Genome: All of the genetic material (the total DNA)
Protein synthesis can be divided into two phases. contained in the chromosomes of an organism
Transcription – A process by which DNA directs the Steps in Transcription Process
synthesis of mRNA molecules
Unwinding of DNA double helix to expose some bases (a
Translation – a process in which mRNA isdeciphered to gene):
synthesize a protein molecule
The unwinding process is governed by RNA polymerase
Differences between RNA and DNA Molecules
Alignment of free ribonucleotides along the exposed DNA
The sugar unit in the backbone of RNA is ribose; it is strand (template) forming new base pairs
deoxyribose in DNA.
RNA polymerase catalyzes the linkage of ribonucleotides
The base thymine found in DNA is replaced by uracil in one by one to form mRNA molecule
RNA
Transcription ends when the RNA polymerase enzyme
RNA is a single-stranded molecule; DNA is double- encounters a stop signal on the DNA template:
stranded (double helix)
The newly formed RNA molecule and the RNA polymerase
RNA molecules are much smaller than DNA molecules, enzyme are released
ranging from 75 nucleotides to a few thousand nucleotides
Post-Transcription Processing: Formation of mRNA
Types of RNA Molecules
Involves conversion of hnRNA to mRNA
Heterogeneous nuclear RNA (hnRNA): Formed directly
by DNA transcription. Splicing: Excision of introns and joining of exons

Post-transcription processing converts the hnRNA to Exon - a gene segment that codes for genetic information
mRNA
Intron – a DNA segments that interrupt a genetic message
Messenger RNA: Carries instructions for protein synthesis
(genetic information) from DNA The splicing process is driven by snRNA

The molecular mass of mRNA varies with the length of the Alternative splicing - A process by which several different
protein protein variants are produced from a single gene
The process involves excision of one or more exons With minor exceptions the code is the same in all
organisms
Transcriptome
The same codon specifies the same amino acid whether
Transcriptome: All of the mRNA molecules that can be the cell is a bacterial cell, a corn plant cell, or a human cell.
generated from the genetic material in a genome.
An initiation codon exists:
Transcriptome is different from a genome
The existence of “stop” codons (UAG, UAA, and UGA)
Responsible for the biochemical complexity created by suggests the existence of “start” codons.
splice variants obtained by hnRNA.
The codon - coding for the amino acid methionine (AUG)
The Genetic Code functions as initiation codon.
The base sequence in a mRNA determines the amino acid Anticodons and tRNA Molecules
sequence for the protein synthesized.
During protein synthesis amino acids do not directly
The base sequence of an mRNA molecule involves only 4 interact with the codons of an mRNA molecule.
different bases - A, C, G, and U
tRNA molecules as intermediaries deliver amino acids to
Codon: A three-nucleotide sequence in an mRNA mRNA.
molecule that codes for a specifi c amino acid
Two important features of the tRNA structure
Based on all possible combination of bases A, G, C, U”
there are 64 possible codes The 3’ end of tRNA is where an amino acid is covalently
bonded to the tRNA.
Genetic code: The assignment of the 64 mRNA codons to
specific amino acids (or stop signals) The loop opposite to the open end of tRNA is the site for a
sequence of three bases called an anticodon.
3 of the 64 codons are termination codons (“stop”
signals) Anticodon - a three-nucleotide sequence on a tRNA
molecule that is complementary to a codon on an mRNA
Characteristics of Genetic Code molecule.
The genetic code is highly degenerate: Translation: Protein Synthesis
Many amino acids are designated by more than one Translation – a process in which mRNA codons are
codon. deciphered to synthesize a protein molecule
Arg, Leu, and Ser - represented by six codons. Ribosome – an rRNA–protein complex - serves as the site
of protein synthesis:
Most other amino acids - represented by two codons
Contains 4 rRNA molecules and ~80 proteins - packed into
Met and Trp - have only a single codon. two rRNA-protein subunits (one small and one large)
Codons that specify the same amino acid are called ~65% rRNA and 35% protein by mass
synonyms
A ribosome’s active site – Large subunit
There is a pattern to the arrangement of synonyms in the
genetic code table. Ribosome is a RNA catalyst
All synonyms for an amino acid fall within a single box in The mRNA binds to the small subunit of the ribosome.
unless there are more than four synonyms
Five Steps of Translation Process
The significance of the “single box” pattern - the first two
bases are the same Activation of tRNA: addition of specific amino acids to the
3’-OH group of tRNA.
For example, the four synonyms for Proline - CCU, CCC,
CCA, and CCG. Initiation of protein synthesis: Begins with binding of
mRNA to small ribosomal subunit such that its first codon
The genetic code is almost universal: (initiating codon AUG) occupies a site called the P site
(peptidyl site)
Elongation: Adjacent to the P site in an mRNA–ribosome Nucleic Acids and Viruses
complex is A site (aminoacyl site) and the next tRNA with
the appropriate anticodon binds to it. Viruses: Tiny disease causing agents with outer protein
envelope and inner nucleic acid core
Termination: The polypeptide continues to grow via
translocation until all necessary amino acids are in place They can not reproduce outside their host cells (living
and bonded to each other. organisms)

Post-translational processing – gives the protein the Invade their host cells to reproduce and in the process
final form it needs to be fully functional disrupt the normal cell’s operation

Efficiency of mRNA Utilizaition Virus invade bacteria, plants animals, and humans:

Polysome (polyribosome): complex of mRNA and several Many human diseases are of viral origin, e. g. Common
ribosomes cold, smallpox, rabies, influenza, hepatitis, and AIDS

Many ribosomes can move simultaneously along a single Vaccines

mRNA molecule
Inactive virus or bacterial envelope
The multiple use of mRNA molecules reduces the amount
of resources and energy that the cell expends to Antibodies produced against inactive viral or bacterial
synthesize needed protein. envelopes will kill the active bacteria and viruses

In the process – several ribosomes bind to a single mRNA Nucleic Acids and Viruses
- polysomes. Viruses attach to the host cell on the outside cell surface
Mutation and proteins of virus envelope catalyze the breakdown of
the cell membrane and forms a hole
An error in base sequence reproduced during DNA
replication Viruses then inject their DNA or RNA into the host cell

Errors in genetic information is passed on during The viral genome is replicated, proteins coding for the viral
transcription. envelope are produced in hundreds of copies.

The altered information can cause changes in amino acid Hundreds of new viruses are produced using the host cell
sequence during protein synthesis and thereby alter replicated genome and proteins in short time
protein function Recombinant DNA and Genetic Engineering
Such changes have a profound effect on an organism. DNA molecules that have been synthesized by splicing a
Mutagens sequence of segment DNA (usually a gene) from one
organism to the DNA of another organism
Mutations are caused by mutagens
Genetic Engineering (Biotechnology):
A mutagen is a substance or agent that causes a change
in the structure of a gene: The study of biochemical techniques that allow the transfer
of a “foreign” gene to a host organism and produce the
Radiation and chemical agents are two important types of protein associated with the added gene
mutagens
Bacterial strains such as E. coli inserted with circular
Ultraviolet, X-ray, radioactivity and cosmic radiation are plasmids, and/or yeast cells carrying vectors containing
mutagenic –cause cancers foreign genes are used for this purpose

Chemical agents can also have mutagenic effects Plasmids (double stranded DNA) replicate independently in
bacteria or yeast
E.g., HNO2 can convert cytosine to uracil
Recombinant DNA Production using a Bacterial
Nitrites, nitrates, and nitrosamines – can form nitrous acid Plasmid
in cells
Dissolution of cells:
Under normal conditions mutations are repaired by
repair enzymes
E. coli cells of a specific strain containing the plasmid of  Deoxynucleotide triphosphates (dATP,
interest are treated with chemicals to dissolve their dGTP, dCTP and dTTP)
membranes and release the cellular contents
 A set of two oligonucleotides with
Isolation of plasmid fraction: complementary sequence to the gene
(primers)
The cellular contents are fractionated to obtain plasmids
 Thermostable plastic container and
Cleavage of plasmid DNA:
 Source of heat
Restriction enzymes are used to cleave the double-
stranded DNA DNA Sequencing

Recombinant DNA Production using a Bacterial  DNA sequencing is a method by which the base
Plasmid sequence in a DNA molecule (or a portion of it) is
determined.
Gene removal from another organism:
 Discovered in 1977 by Fredrick Sanger
Using the same restriction enzyme the gene of interest is
removed from a chromosome of another organism  Concept in DNA sequencing:

Gene–plasmid splicing:  Selective interruption of polynucleotide synthesis

using 2’,3’-dideoxyribonucleotide triphosphates
The gene (from Step 4) and the opened plasmid (from (ddNTPs).
Step 3) are mixed in the presence of the enzyme DNA
ligase to splice them together.  This interruption of synthesis leads to the formation
of every possible nucleotide site mixture.
Uptake of recombinant DNA:
 These nucleotides are labeled using radioactive
The recombinant DNA prepared in stept 5 are transferred dNTP during their synthesis.
to a live E. coli culture where they can be replicated,
trasncribed and translated.  The radiolablled nucleotides are then separated on
a gel by electrophoresis
Recombinant DNA and Genetic Engineering
 Basic steps involved in DNA Sequencing
Transformed cell can reproduce a large number of identical
cells –clones:  Step 1: Cleavage of DNA using restriction
enzymes: Restriction enzymes are used to cleave
Clones are the cells that have descended from a single cell the large DNA molecule into smaller fragments
and have identical DNA (100–200 base pairs).
Given bacteria grow very fast, within few hours 1000s of  Step 2: Separation into individual components:
clones will be produced The mixture of small DNA fragments generated by
the restriction enzymes is separated into individual
Each clone can synthesize the protein directed by foreign components via gel electrophoresis techniques.
gene it carries
 Step 3: Separation into single strands: A given
Polymerase Chain Reaction DNA fragment is separated into its two strands by
The polymerase chain reaction (PCR) is a method for chemical methods to use it as a template in step 4.
rapidly producing multiple copies of a DNA nucleotide Vitamins and minerals
sequence (gene).
Characteristics of minerals
This method allows to produce billions of copies of a
specific gene in a few hours. • Organic compounds
PCR is very easy to carryout and the requirements are: • Must be obtained from dietary sources
 Source of gene to be copied • Human body can’t synthesize in enough amounts
 Thermostabel DNA polymerase • Essential for proper functioning of the body

• Needed in micro and milligram quantities

 • 1 Gram of vitamin B is sufficient for 500,000 people Vitamins A, D, E, K

• Enough vitamin can be obtained from balanced diet • Involved in plasma membrane processes

• Supplemental vitamins may be needed after illness • More hydrocarbon like with fewer functional groups

• Many enzymes contain vitamins as part of their • Vitamin A

structures - conjugated enzymes
– Has role in vision - only 1/1000 of vitamin A is
• Two Classes in retina

– Water Soluble and Fat Soluable – 3 Forms of vitamin A are active in the body

• Synthetic and natural vitamins are same – Derived from b-carotine

– 13 Known vitamins Functions of Vitamin A

Vitamin C • Vision: In the eye- vitamin A combines with opsin

protein to form the visual pigment rhodopsin which
• Humans, monkeys, apes and guinea pigs need further converts light energy into nerve impulses that
dietary vitamins are sent to the brain.
• Co-substrate in the formation of structural protein • Regulating Cell Differentiation - process in which
collagen immature cells change to specialized cells with
function.
• Involved in metabolism of certain amino acids
– Examples: Differentiation of bone marrow
• 100 mg/day saturates all body tissues - Excess cells white blood cells and red blood cells.
vitamin is excreted
• Maintenance of the healthy of epithelial tissues via
• RDA (mg/day): epithelial tissue differentiation.
– Great Britain: 30 – Lack of vitamin A causes such surfaces to
– United States and Canada: 60 become drier and harder than normal.

– Germany: 75 • Reproduction and Growth: In men, vitamin A

participates in sperm development. In women,
Vitamin B normal fetal development during pregnancy requires
vitamin A.
• The preferred and alternative names for the B
vitamins Vitamin D

• Thiamin (vitamin B1) • Two forms active in the body: Vitamin D2 and D3

• Riboflavin (vitamin B2) • Sunshine Vitamin: Synthesized by UV light from sun

• Niacin (nicotinic acid, nicotinamide, vitamin B3) • It controls correct ratio of Ca and P for bone
mineralization (hardening)
• Vitamin B6 (pyridoxine, pyridoxal, pyridoxamine)
• As a hormone it promotes Ca and P absorption in
• Folate (folic acid) intestine

• Vitamin B12 (cobalamin) Vitamin E

• Pantothenic acid (vitamin B5) • Four forms of Vitamin Es: a-, b-, g- and d-Vitamin E

• Biotin • Alpha-tocopherol is the most active biological active

form of Vitamin E
• Exhibit structural diversity
• Peanut oils, green and leafy vegetables and whole
• Major function: B Vitamins are components of grain products are the sources of vitamin E
coenzymes
 • Primary function: Antioxidant – protects against • Functions: Maintains water balance in the body and
oxidation of other compounds controls body temperature, helps you sweat when
body temperature rises
Vitamin K
• Sources: Cheese, smoked meats, fish, table salt,
• Two major forms; K1 and K2
• Deficiency: deficiency is highly unlikely
• K1 found in dark green, leafy vegetables
Potassium
• K2 is synthesized by bacteria that grow in colon
• Functions: Muscle contraction and in maintaining
• Dietary need supply: ~1/2 synthesized by bacteria body fluid. It is necessary for the building of muscle
and 1/2 obtained from diet and for normal body growth.
• Active in the formation of proteins involved in • Sources: Banana, celery, meat, fruits, milk, grains,
regulating blood clotting legumes, raisins, dates, figs
Unlike vitamins which are organic substances, minerals are
• • Deficiency: dry skin, acne, muscle spasms or
inorganic substances which is needed in small amounts that weakness
must be obtained from food Zinc

Minerals can be divided into two groups – those needed in • Functions: Aids the immune system. Cofactor in
• enzymes. Needed for the senses of smell and taste
large quantities (Major minerals) and those only required in tiny
amounts (trace elements)
• Sources: Meat esp. lamb meat, oats, eggs, nuts

• Deficiency: Retarded growth

IRON
• Excess: Enlarged liver
• Functions: Production of hemoglobin in red blood
cells to carry oxygen in the blood Iodine

• Sources: Red meat, liver, eggs, bread, green • Functions: Thyroid gland function (controls how
vegetables quickly the body uses energy) and body metabolism

• Deficiency: Anemia • Sources: Milk, eggs, yogurt, seafood, iodized salt

Calcium • Disease involved Goiter

• Functions: Teeth and bones, blood clotting, nerve Magnesium

and muscle contraction, heart regulation
• Functions: muscle contraction, DNA synthesis,
• Sources: Dairy products, fortified white bread, green controls blood sugar and blood pressure, cofactor of
vegetables, nuts and seeds enzymes

• Deficiency: Stunted growth can cause rickets and • Sources: Cheeses, cocoa, chocolate, nuts, beans
osteoporosis
• Deficiency: hypocalcemia
Phosphorus

• Functions: Bones and teeth accompanied by

calcium, muscle contraction

• Sources: Dairy products, nuts, meat, fish, oats,

cocoa

• Deficiency: rarely deficient but could cause tiredness

and depression

Sodium