PROTEINS

BIOCHEMISTRY
CHAPTER 2
N E T I P O R
P R O T E I N
N E YMS E Z
E N Z YME S
NOM I A
C D A I
AM I NO
A C I D
Role of Protein
• Some carry out the transport and storage
of small molecules.
• Others make up a large part of the
structural framework of cells and tissues.
• Muscle contraction, the immune
response and blood clotting are all
mediated.
Amino acids
• Building blocks that are found in all proteins.

POLYMER MONOMER

PROTEINS α - AMINO ACIDS

Zwitterion
Chiral
• 4 different substituent attach to the carbon.

ALANINE GLYCINE
How many chiral centers
are there in isoleucine?

A. 1
B. 2
C. 3
D. 4
Fischer Projection

• A Fischer projection or
Fischer projection formula
is a convention used to
depict a stereoformula in
two dimension without
destroying the
stereochemical
information, i.e., absolute
configuration, at chiral
centers.
If a molecule contains one asymmetric carbon,
two distinguishable stereoisomers exists.
 Enantiomer
s
• Also called optical
isomers – polarized
light in opposite
direction
• Non superimposabl
e
mirror images of
one another.
 20
Common
Amino
Acids
 Hydrophobic

Aliphatic Amino Acids

Cyclic Amino
Acids
• Has a primarily aliphatic
character
• Frequently found on the
surfaces of proteins dues
to its unique structural
constraints.
• Sites in a protein structure
where protein must fold
back to itself (turns)
Amino Acids with hydroxyl/sulfur
containing side chain

More Hydrophilic Character

Aromatic Amino Acids

Most hydrophobic amino acids

 Basic Amino Acids

Are strongly polar and

as a consequence, they
are usually found on
the exterior surfaces of
proteins. They can be
hydrated by the
surrounding aqueous
environment.
Acidic Amino Acids

hydrophilic
• Oligopeptides – consists of only a few amino acids (between
two and twenty). Includes dipeptides, tripeptides, and
tetrapeptides

• Polypeptides- more than 20

• Protein- Larger polypeptides or more than one polypeptide.

Greater than 50
Coenzymes are organic compounds required by many
enzymes for catalytic activity. They are often vitamins, or
derivatives of vitamins. Sometimes they can act as catalysts in
the absence of enzymes, but not so effectively as in
conjunction with an enzyme.

Examples of coenzymes: nicotineamideadenine

dinucleotide (NAD), nicotineamide adenine
dinucelotide phosphate (NADP), and flavin adenine
dinucleotide (FAD). These three coenzymes are
involved in oxidation or hydrogen transfer.