Proteins are very
important in biological systems as control and structural elements. Control
functions of proteins are carried out by enzymes and proteinaceous hormones.
Enzymes are chemicals that act as organic catalysts (a catalyst is a chemical
that promotes but is not changed by a chemical reaction).
Proteins Basic Units:
The building block of any protein is the
amino acid, which has an amino end (-NH2)
and a carboxyl end (-COOH). The structure of a generalized amino acid as well
as the specific structures of the 20 biological amino acids are shown in Figure
1 and 2 respectively.
The R indicates
the variable component (R-group) of each amino acid. Alanine and
Valine, for example, are both nonpolar amino acids, but they differ,
as do all amino acids, by the composition of their R-groups. All living things
(and even viruses) use various combinations of the same twenty amino acids. A
very powerful bit of evidence for the phylogenetic connection of all living
things.
Amino acids are
linked together by joining the amino end of one molecule to the carboxyl end of
another. Removal of water allows formation of a type of covalent bond known as
a peptide bond. This process is illustrated in Figure 3.
Figure 3. Formation of a
peptide bond between two amino acids by the condensation (dehydration) of the
amino end of one amino acid and the acid end of the other amino acid.
Proteins
and their Organization :
Amino acids are linked
together into a polypeptide, the primary structure in the organization of
proteins. The primary structure of a protein is the sequence of amino acids,
which is directly related to the sequence of information in the RNA molecule,
which in turn is a copy of the information in the DNA molecule.
Changes in the primary
structure can alter the proper functioning of the protein. Protein function is
usually tied to their three-dimensional structure.
The primary structure is the
sequence of amino acids in a polypeptide..The secondary structure is
the tendency of the polypeptide to coil or pleat due to H-bonding between
R-groups. The tertiary structure is controlled by bonding (or
in some cases repulsion) between R-groups.
Tertiary structure of an HIV
protein and its similarity to gamma interferon are shown in Figure 4. Many
proteins, such as hemoglobin, are formed from one or more polypeptides. Such
structure is termed Quaternary structure.
Structural
proteins, such as collagen, have regular repeated primary structures. Like the
structural carbohydrates, the components determine the final shape and
ultimately function.
·
Collagens have a variety of functions in living things,
such as the tendons, hide, and corneas of a cow.
·
Keratin is another structural protein. It is found in
fingernails, feathers, hair, and rhinoceros horns.
·
Microtubules, important in cell division
and structures of flagella and cilia (among other things), are composed of
globular structural proteins.
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