Protein Structure
What are Proteins Made Of?
All proteins are made up of alpha amino acids. A picture of an amino acid
is shown below.
In this picture you have a carbon with an R group on it bonded to an
amid and a caboxyl on each side. There are different
R groups on the 20 common amino acids that are incorporated into proteins.
These groups include some straight chains, aromatic groups, acids, and
bases. Some of these groups bind quite well to water, these are the hydrophilic
groups. Others do not bind at all to water, these are called hydrophobic
groups. The stereochemistry of amino acids are important. All amino acids
can exist in D and L forms. Amino acids incorporated into protein structures
are of the L form.
How do These Amino Acids Bind Together?
Amino acids link together between the amide and carboxyl groups. Two amino
acids bind together and eliminate water resulting in a peptide
link. What is left is referred to as an amino acid residue. If this
chain becomes very long, it is then called a polypeptide. All proteins
are polypeptides of a defined sequence of amino acids.
Structures a Protein can Take
There are four different structures a protein can have. The first structure
is primary structure. This is just a chain of amino acids linked together.
Secondary structure results from hydrogen binding between the amide and
the carboxyl of groups that are not very far apart on the backbone of the
protein. This can make structures such as alpha
helicies, beta sheets, and beta turns. Then there is tertiary
structure. This is largely due to packing of the elements of secondary
structure against one another. Here hydrophobic groups tend to stay close
together. This is also true for hydrophilic groups. Usually hydrophobic
groups pack closely in the center of the protein while the hydrophilic
groups surround this hydrophobic center. This is because proteins are usually
found in water. Finally, there is quaternary
structure. This is where folded polypeptide chains interact with each
other. All of the structures except primary structure depend on intermolecular
forces.
Why is This so Important?
Not only the chemical structure is important, but its physical structure
is just as important when you are determining the activity of the protein.
This means that when you precipitate a protein, you can not do anything
to change the physical structure. Examples of how a protein gets damaged
or denatured
are the addition of too much salt, or the pH of the solution becomes extremely
acidic. Proteins are sensitive at low pH. This makes them more sensitive
to anions in an acid or a salt in the solution.
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