Chemistry

Project

Anushka K.C.
Abhishek K.C.
Abhishek Giri
Aditya Parajuli
Akar Shrestha

PROTEINS

Topic Preview:
I.

Amino Acids
II. Proteins
III. Structure of Proteins

Amino Acids

Amino Acids are the building units of proteins.

Proteins are polymers of amino acids linked together by Peptide bond.
There are about 300 amino acids that occur in nature. Only 20 of them occur
in proteins.
Structure of amino acids: Each amino acid has 4 different groups attached to
- carbon (which is C-atom next to COOH). These 4 groups are: amino group,
COOH group, Hydrogen atom and side chain (R)

 The amino group of one

molecule condenses with the
acid group of another.

Zwitterion
Amino acid exists as a dipolar ion.
-COOH loses H+, -NH2 gains H+.

In acidic conditions amino acids become positively charged

In alkaline conditions they become negatively charged
Actual structure depends on pH.

Proteins

Proteins are formed by condensation polymerization

The polypeptide chain in proteins are unbranched
Each protein has a unique sequence of amino acids
The sequence of amino acids are determined by DNA
Each protein has a particular biological function

Protein Structures
1. Primary
2. Secondary
3. Tertiary
4. Quaternary

Primary Structure
A sequence
of amino acids in a
polypeptide chain.
The most common way to
denote a primary structure
is to write the amino acid
sequence using the
standard three-letter
abbreviations for the amino
acids. For example: gly-glyser-ala

Secondary Structure
Secondary structure is the ordered
arrangement or conformation of
amino acids in localized regions of a
polypeptide or protein molecule.
Hydrogen bonding plays an
important role in stabilizing these
folding patterns.

. The two main secondary structures

are the alpha helix and the antiparallel beta-pleated sheet.
There are other periodic
conformations, but the -helix and
-pleated sheet are the most stable.
A single polypeptide or protein may
contain multiple secondary
structures.

 Alpha Helix

Each carbonyl oxygen can hydrogen bond with an N-H hydrogen on the
next turn of the coil.

 Beta-Pleated Sheet
Each carbonyl oxygen hydrogen bonds with an N-H hydrogen on
an adjacent peptide chain.

Tertiary Structure
The tertiary structure of a polypeptide or protein is
the three-dimensional arrangement of the atoms
within a single polypeptide chain.
For a polypeptide consisting of a single
conformational folding pattern (e.g., an alpha helix
only), the secondary and tertiary structure may be
one and the same.
Tertiary structure is largely maintained by disulfide
bonds. Disulfide bonds are formed between the side
chains of cysteine by oxidation of two thiol groups
(SH) to form a disulfide bond (S-S), also sometimes
called a disulfide bridge.
There are also other bonds that stabilize the 3-D
shape:
Van der Waals forces
Hydrogen bonds
Ionic bonds

In Summary

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