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Overview of Proteins and Amino Acids

Proteins are made up of amino acids and perform many important functions in living organisms. They can be classified based on their structure and properties. Some key points covered are that proteins have primary, secondary, tertiary and quaternary structure. Essential amino acids cannot be made by the body and must come from food. Common protein functions include enzymes, hormones, structural roles, and immune defense.

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36 views41 pages

Overview of Proteins and Amino Acids

Proteins are made up of amino acids and perform many important functions in living organisms. They can be classified based on their structure and properties. Some key points covered are that proteins have primary, secondary, tertiary and quaternary structure. Essential amino acids cannot be made by the body and must come from food. Common protein functions include enzymes, hormones, structural roles, and immune defense.

Uploaded by

Arbaan Hashmi
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PPTX, PDF, TXT or read online on Scribd

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Proteins
Introduction
 In 1839 dutch chemist Gerardus Johannes mulder
while invesitgating substances such as those found
in milk,egg foud that they could be coagulated on
heating and these were nitrogenous compounds.
 Swedish scientist Jons Jacob berzelius suggested to
Mulder that these substances should be called
proteins.
Proteins
 Proteins are the nitrogeneous colloidal
substances made up of amino acids
residue joined together by peptide linkage.
 Proteins are large biological molecules
consisting of one or more chains of amino
acids.
 Proteins perform a vast array of functions
within living organisms, including
catalyzing metabolic reactions, replicating
DNA, responding to stimuli, and
transporting molecules from one location
to another.
Amino acid
 Amino acids are chemical compounds
containing carbon, hydrogen, oxygen and
nitrogen, which combine together into
different structures to form the various
types of protein that the body requires.
 There are many forms of protein, which
all play an important role in the function
of the body. For example, collagen is a
protein and is vital for the strength,
elasticity and composition of our hair and
skin.
Classification of amino acids

AMINO ACIDS

PROTEIN FORMING NON-PROTEIN FORMING

ESSENTIAL NON-ESSESNTIAL
AMINO ACIDS AMINO ACIDS

SPECIAL AMINO ACIDS


Classification of amino acids on the basis of
reaction
 Neutral
These are simple monoamino monocarboxylic acids
Aliphatic,Aromatic,Heterocyclic and S- containing
Amino acids.
 Acidic
These amino acids have two carboxyl group and one
amino group.
 Basic
These amino acids have one carboxyl group and two
amino group.
Essential amino acids
 Metheonine
 Arginine ( semi-essntial )
 Threonine
 Tryptophan
 Valine
 leucine
 Isoleucine
 Phenylalanine
 Histidine ( semi-essential )
 Lysine
Non-Essential amino acids
 Alanine
 Aspargine
 Aspartic acid
 Cysteine
 Glutamic acid
 Glycine
 Hydroxyline
 Proline
 Serine
 Tyrosine
Special amino acids

 Citruline
 Ornithine
 Taurine
 DOPA
 GABA
Classification of protein forming amino acids on the basis of
their side chain & functional group

 Mono-amino mono carboxylic


( neutral amino acids )
 Mono-amino Dicarboxylic
( acidic amino acids )
 Di-amino mono carboxylic
( basic amino acids )
 Imino acids
ARGININE (SE)

 can be made by the body in adults but not in sufficient


amounts in children
 supports and speeds up wound healing / tissue repair
 strengthens the immune system
 promotes the release of hormones
 helps to reduce blood pressure
 precursor to nitric oxide (NO)
HISTIDINE (SM)
 It is a precursor to histamine, which stimulates chloric acid
production in the stomach.
 Supports healthy growth and promotes tissue repair
 Important for conversion of glucose into glycogen by the liver;
hence, supports blood sugar regulation
 Necessary for hemoglobin formation in red blood cells, as well
as proper storage and movement of iron, thus helping to ward off
anemia
 Serves as an important antioxidant, and thus promotes
cardiovascular health
ISOLEUCINE (E)
 It is a branched-chain amino acid
 It is necessary for hemoglobin formation
 It helps to regulate blood sugar
 It promotes muscle recovery after physical
exercise
 It provides fuel for muscle work
LEUCINE (E)
 It is also branched-chain amino acid
 supports and speeds up tissue repair / wound
healing
 It is necessary for growth hormone production
 helps to regulate blood sugar
 promotes muscle recovery after physical exercise
LYSINE (E)
 supports healthy growth and bone
development in children
 promotes calcium absorption
 important in the production of enzymes,
hormones, and antibodies
 supports and speeds up tissue repair
 provides fuel for muscle work
METHIONINE (E)

 It facilitates lipid (fat) metabolism healthy

digestion, blood lipid regulation

 It is important in heavy metal detoxification

 It is an important antioxidant

 It is initiator of protien synthesis


PHENYLALANINE (E)

 It is a precursor to tyrosine

 It is potentially helpful for chronic pain,

Parkinson’s, and mood disorders


THREONINE (E)
 It is a precursor to isoleucine
 it can be transformed by the body into glycine
 It promotes healthy thymus growth and function, thus
contributing to a healthy immune system
 It participates in antibody formation to ward off
infections and promote speedy recovery
 It is important to lipid (fat) metabolism and
regulation
TRYPTOPHAN (E)
 It is a precursor to niacin and serotonin

(neurotransmitter)

 It promotes mental health and well being

 It is helpful for children/adults with ADHD

(Attension deficit hyperactive disorder)

 facilitates sleep
VALINE (E)
 It is a branched amino acid.
 It provides fuel for muscle work
 It is vital for healthy muscle tissue and tissue repair
 It is helpful with alcohol related liver damage
and hepatic encephalopathy (Hepatic coma) , as
well as degenerative neurological illness
ALANINE (NE)

 supports glucose metabolism

 It helps to maintain a healthy nitrogen balance

 It is an important component of collagen


ASPARAGINE (NE)

 It helps to keep the central nervous system healthy

 It helps you to maintain your equilibrium/balance

 It plays an important role in changing one amino

acid into another (transamination)


Continue..(NE)

Glycine
 Conjuugate with cholic acid to synthesize Na-
glychocholate( bile salts )
 Takes part in the synthesis of glutathion.
 It is glucogenic.
Aspartic acid
 Takes part in the synthesis of purines & pyrimidines
bases for nucliec acids.
Glutamic acid
 Takes part in the synthesis of glutathion.
Continue..
Phenylalanine (E)
 Synthesize tyrosine,DOPA & nor-adrenaline
Tyrosine (NE)
 Synthesize thyroid hormone
 Synthesize melanin
Tryptophan (E)
 60 mg of tryptophan in the body produces 1 mg of niacin.
 Synthesize serotonin
Protein structure
 The structure of proteins are organized at four
different level.
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure
Primary structure
 The number and order

of amino acids in the

straight polypeptide

chains is called primary

structure of the proteins.


Secondary structure
 The folding of
polypeptide chains into a
specific coiled structure
held together by
disulfide and hydrogen
bonds is called the
secondary structure.
Tertiary structure

 The arrangemet and

interrelation-ship of the

coiled chains of proteins into

specific layers or fibers is

called tertiary structure.


Quaternary structure
 Several monomeric
units each with
appropriate
priamary,secondry &
tertiary structure may
combine together the
association of similar or
dissimiliar subunits is
called quaternary
structure.
Functions of proteins
1. All the enzymes are proteins.

2. Some hormones are proteins e.g insulin,glucgon.


3. Perform carrier function e.g hemoglobin
4. Help in coagulation of blood e.g fibrinogen
5. Provides defense to the body e.g immuoglobulins.
6. Help in contraction of muscles e.g actin & myosin
Classification of proteins

1. Physio-chemical classification

2. Functional classification

3. Structural classification
Phsyio-chemical classification

1. Simple proteins

2. Compound proteins

3. Derived proteins
Simple Proteins

1. Albumins

2. Globulins

3. Glutelins

4. Histories

5. Protamine

6. prolamines

7. Scleroproteins
Conjugated Proteins

1. Glycoproteins
2. Chromoproteins
3. Lipproteins
4. Nucleoproteins
5. Phosphoprotein
Functional classification

1. Catalytic proteins

2. Regulatory proteins

3. Structural proteins
4. Transport proteins

5. Defensive proteins

6. Contractile proteins
7. Genetic proteins

8. Storage proteins
Structural classification

1. Globular proteins

2. Fibrous proteins
Structural classification
Fibrous Proteins
 Little or no tertiary structure.
 Long parallel polypeptide chains.
 Cross linkages at intervals forming long fibres or sheets.
 Usually insoluble.
 Many have structural roles.
 E.g. keratin in hair and the outer layer of skin, collagen (a
connective tissue).

Globular Proteins
 Have complex tertiary and sometimes quaternary structures.
 Folded into spherical (globular) shapes.
 Usually soluble as hydrophobic side chains in centre of structure.
 Roles in metabolic reactions.
 E.g. enzymes, haemoglobin in blood.
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