WHAT CONDITIONS CAN DENATURE PROTEINS?
What Is Protein Denaturation?
Living organisms require many types of large molecules in order to survive. Very
few of these molecules serve as many purposes as proteins. Proteins are large
molecules composed of folded chains of amino acids. Every protein has a
unique shape and that shape determines the things it does. You could think of
them as keys that fit into certain locks around the body.
Proteins do lots of different things around the body, including speeding up
biological processes, recognizing antibodies, providing structure to certain body
parts, transporting substances, regulating genes, and responding to signals
inside and outside the body.
Proteins range in size from small ones, such as insulin - only 51 amino acids long,
to extremely large ones, such as titin - almost 27,000 amino acids long. No
matter their size, they must be folded into a particular shape in order to function.
Sometimes, though, things go wrong and cause the protein to
unfold. Denaturation is the process by which proteins lose their folded structure
and cease to function.
The Structure of Proteins: Primary Structure
Every protein has four levels of structure which scientists refer to. The four levels
are primary, secondary, tertiary, and quaternary.
The primary structure of a protein is the sequence of amino acids that form that
protein. Every protein has a unique sequence of amino acids linked together in
a long chain. If the amino acids are out of order, the protein will not function
properly.
For example, insulin has a chain which begins with the amino acid glycine,
followed by isoleucine,valine , and glutamic acid. The chain continues, but you
get the idea. If any members of this chain are out of order - for example, if the
glycine was switched with the valine, then the resulting chain wouldn't combine
to insulin. It's only because the amino acids are linked this way that insulin is
created
LIPID BILAYER PERMEABILITY
All living cells must be able to exchange materials (nutrients and waste products)
with their external environments in order to remain alive. Because the
phospholipid bilayer is responsible for forming membranes and hence
compartments, it is important to understand how various molecules can pass
through this lipid bilayer. Simply stated, biological membranes
are semipermeable lipid bilayers. Permeability refers to the ease with which
molecules cross biological membranes. Because of the chemical and structural
nature of the phospholipid bilayer (hydrophobic core), only lipid-soluble
molecules and some small molecules are able to freely pass through the lipid
bilayer. Ions and large polar molecules cannot pass through the lipid bilayer. But
more specifically, whether a molecule can pass through the membrane depends
on its size and its electrical nature. The membrane is highly permeable to non-
polar (fat-soluble) molecules. The permeability of the membrane to polar (water
soluble) molecules is very low, and the permeability is particularly low to large
polar molecules. The permeability to charged molecular species (ions) is very low.
Therefore, the passage of most molecules and ions is aided by the presence of
specific membrane transport proteins.
The proper way to state these features is to say that the membrane is
highly permeable to lipid-soluble molecules, or that the membrane is
not permeable to ions. It may also be said that membrane permeability is high for
lipid-soluble molecules, and that membrane permeability is low for ions and polar
molecules. Another way of stating this is that lipid-soluble molecules are
highly permeant, or that ions are impermeant (i.e., not permeant).
Carrier proteins transfer an ion or a molecule from one side of a membrane to
the other. They are specific to each ion or molecular species. While the
movement of the ion or molecule itself is passive, the motive force for the carrier
protein is provided by the proton or pH gradient and/or electrical gradient,
which are set up by the proton pumps (see below). Carrier proteins may act as
“symporters,” transferring two different species across the membrane in the
same direction, or as “antiporters,” which transfer one species in one direction
and the other in the opposite direction.
Carrier Proteins
Carrier proteins bind a solute on one side of the membrane and deliver it to the
other side through a change in conformation. The transported solutes may be
small organic molecules or inorganic ions. Their transport may be passive, down
their electrochemical gradient, or actively coupled to the electrochemical
gradient of another solute. Carrier proteins are often highly selective, and the
complement of carrier proteins in a particular membrane is uniquely specialized
to the requirements of the compartment that the membrane surrounds. In
the plasma membrane there are carriers to import inorganic ions and nutrients
such as sugars and amino acids. Since these must frequently be accumulated
against their electrochemical gradient, their transport is generally coupled to
the H+ electrochemical gradient by a symport mechanism. In the tonoplast,
carrier proteins serve to remove cytotoxic solutes, such as Na+ and Ca2+, from
the cytoplasm. Again the transport of these ions is coupled to the
H+ electrochemical gradient, but by an antiport mechanism. A variety of carrier
proteins are present on the inner membranes of mitochondria and chloroplasts.
These are required for the specific biochemistry of these organelles.
NAME: Kemuel R. Lozada
SECTION: Grade11B Prudence
