INTRODUCTION

A living system grows, sustains and reproduces itself. The most amazing
thing about a living system is that it is composed of non-living atoms
and molecules. The pursuit of knowledge of what goes on chemically
within a living system falls in the domain of biochemistry. Living
systems are made up of various complex biomolecules like
carbohydrates, proteins, nucleic acids, lipids, etc. Proteins and
carbohydrates are essential constituents of our food. These biomolecules
interact with each other and constitute the molecular logic of life
processes. In addition, some simple molecules like vitamins and mineral
salts also play an important role in the functions of organisms. Structures
and functions of some of these biomolecules
 Proteins

Proteins are large biomolecules and macromolecules that comprise one

or more long chains of amino acid residues. Proteins perform a vast
array of functions within organisms, including catalysing metabolic
reactions, DNA replication, responding to stimuli, providing structure to
cells and organisms, and transporting molecules from one location to
another. Proteins differ from one another primarily in their sequence of
amino acids, which is dictated by the nucleotide sequence of their genes,
and which usually results in protein folding into a specific 3D
structure that determines its activity.
A linear chain of amino acid residues is called a polypeptide. A protein
contains at least one long polypeptide. Short polypeptides, containing
less than 20–30 residues, are rarely considered to be proteins and are
commonly called peptides. The individual amino acid residues are
bonded together by peptide bonds and adjacent amino acid residues.
The sequence of amino acid residues in a protein is defined by
the sequence of a gene, which is encoded in the genetic code. In general,
the genetic code specifies 20 standard amino acids. Shortly after or even
during synthesis, the residues in a protein are often chemically modified
by post-translational modification, which alters the physical and
chemical properties, folding, stability, activity, and ultimately, the
function of the proteins. Some proteins have non-peptide groups
attached, which can be called prosthetic groups or cofactors. Proteins
can also work together to achieve a particular function, and they often
associate to form stable protein complexes.
 Biochemistry

Most proteins consist of linear polymers built from series of up to 20

different L-α- amino acids. All proteinogenic amino acids possess
common structural features, including an α-carbon to which
an amino group, a carboxyl group, and a variable side chain are bonded.
Only proline differs from this basic structure as it contains an unusual
ring to the N-end amine group, which forces the CO–NH amide moiety
into a fixed conformation. The side chains of the standard amino acids,
detailed in the list of standard amino acids, have a great variety of
chemical structures and properties; it is the combined effect of all of the
amino acid side chains in a protein that ultimately determines its three-
dimensional structure and its chemical reactivity. The amino acids in a
polypeptide chain are linked by peptide bonds. Once linked in the
protein chain, an individual amino acid is called a residue, and the linked
series of carbon, nitrogen, and oxygen atoms are known as the main
chain or protein backbone.
 Structure And Its Types

Most proteins fold into unique 3D structures. The shape into which a

protein naturally folds is known as its native conformation.   Although
many proteins can fold unassisted, simply through the chemical
properties of their amino acids, others require the aid of
molecular chaperones to fold into their native states.   Biochemists often
refer to four distinct aspects of a protein's structure:  

 Primary structure: the amino acid sequence. A protein is a polyamide.

 Secondary structure: regularly repeating local structures stabilized
by hydrogen bonds. The most common examples are the α-helix, β-
sheet and turns. Because secondary structures are local, many regions
of different secondary structure can be present in the same protein
molecule.
 Tertiary structure: the overall shape of a single protein molecule; the
spatial relationship of the secondary structures to one another.
Tertiary structure is generally stabilized by nonlocal interactions,
most commonly the formation of a hydrophobic core, but also
through salt bridges, hydrogen bonds, disulfide bonds, and
even posttranslational modifications. The term "tertiary structure" is
often used as synonymous with the term fold. The tertiary structure is
what controls the basic function of the protein.
 Quaternary structure: the structure formed by several protein
molecules (polypeptide chains), usually called protein subunits in this
context, which function as a single protein complex.
 Protein primary structure

Protein primary structure is the linear sequence of amino acids in

a peptide or protein. By convention, the primary structure of a protein is
reported starting from the amino-terminal (N) end to the carboxyl-
terminal (C) end. Protein biosynthesis is most commonly performed
by ribosomes in cells. Peptides can also be synthesized in the laboratory.
Protein primary structures can be directly sequenced, or inferred
from DNA sequences.
 Protein secondary structure

Protein secondary structure is the three dimensional form of local

segments of proteins. The two most common secondary structural
elements are alpha helices and beta sheets, though beta turns and omega
loops occur as well. Secondary structure elements typically
spontaneously form as an intermediate before the protein folds into its
three dimensional tertiary structure.
Secondary structure is formally defined by the pattern of hydrogen
bonds between the amino hydrogen and carboxyl oxygen atoms in the
peptide backbone. Secondary structure may alternatively be defined
based on the regular pattern of backbone dihedral angles in a particular
region of the Ramachandran plot regardless of whether it has the correct
hydrogen bonds.
 Types of Secondary Proteins

The most common secondary structures are alpha helices and beta

sheets. Other helices, such as the 310 helix and π helix, are calculated to
have energetically favorable hydrogen-bonding patterns but are rarely
observed in natural proteins except at the ends of α helices due to
unfavorable backbone packing in the center of the helix. Other extended
structures such as the polyproline helix and alpha sheet are rare in native
state proteins but are often hypothesized as important protein
folding intermediates. Tight turns and loose, flexible loops link the more
"regular" secondary structure elements. The random coil is not a true
secondary structure, but is the class of conformations that indicate an
absence of regular secondary structure.
Amino acids vary in their ability to form the various secondary structure
elements. Proline and glycine are sometimes known as "helix breakers"
because they disrupt the regularity of the α helical backbone
conformation; however, both have unusual conformational abilities and
are commonly found in turns. Amino acids that prefer to
adopt helical conformations in proteins
include methionine, alanine, leucine, glutamate and lysine ; by contrast,
the large aromatic residues (tryptophan, tyrosine and phenylalanine) and
Cβ-branched amino acids (isoleucine, valine, and threonine) prefer to
adopt β-strand conformations. However, these preferences are not strong
enough to produce a reliable method of predicting secondary structure
from sequence alone.
 Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein.

The tertiary structure will have a single polypeptide chain "backbone"
with one or more protein secondary structures, the protein
domains. Amino acid side chains may interact and bond in a number of
ways. The interactions and bonds of side chains within a particular
protein determine its tertiary structure. The protein tertiary structure is
defined by its atomic coordinates. These coordinates may refer either to
a protein domain or to the entire tertiary structure. A number of tertiary
structures may fold into a quaternary structure
 Protein quaternary structure

Protein quaternary structure is the fourth (and highest) classification

level of protein structure. Protein quaternary structure refers to the
structure of proteins which are themselves composed of two or more
smaller protein chains (also referred to as subunits). Protein quaternary
structure describes the number and arrangement of
multiple folded protein subunits in a multi-subunit complex. In contrast
to the first three levels of protein structure, not all proteins will have a
quaternary structure since some proteins function as single units. Protein
quaternary structure can also refer to biomolecular complexes of
proteins with nucleic acids and other cofactors.
Bibliography & Vote of Thanks