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Lec3 Part 2

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8 views32 pages

Lec3 Part 2

Uploaded by

iayatoo678
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Amino acids and

Proteins chemistry

(2)
Non-standard amino acids
Besides the 20 amino acids present in protein
structure, there are several other amino acids which
are biologically important.
I. Amino acid derivatives: e.g.
 Hydroxyproline and hydroxylsine (present in
collagen).

 Methylated or phosphorylated amino acids (present


in histones of DNA).
6-N-Methyllysine

is a constituent of myosin, a contractile protein of


muscle.
Carboxyglutamate

found in the blood clotting protein prothrombin.


More complex is desmosine
a derivative of four Lysine residues, which is found in
the fibrous protein elastin.
Selenocysteine

This rare amino acid residue is introduced during


protein synthesis. It contains selenium rather than the
sulfur of cysteine. Actually derived from serine.
II. Non-protein amino acids: Ornithine, Citrulline
and DOPA.

Ornithine Citrulline

They are key intermediates (metabolites) in the


biosynthesis of arginine and in the urea synthesis.
DOPA is an intermediate in the synthesis of
epinephrine from tyrosine.
The Peptide Bond
Peptide bond formation is a condensation reaction
leading to the polymerization of amino acids into
peptides and proteins.
Peptides are small, consisting of few amino acids.
Enzymes, many hormones, antibodies and
neurotransmitters are peptides.
Proteins are polypeptides of greatly divergent length
and amino acid composition.
• The simplest peptide, a dipeptide, containing a
single peptide bond formed by the
condensation of the carboxyl group of one
amino acid with the amino group of the second
amino acid with the concomitant elimination
of water.
• Several amino acids can be condensed in the
same fashion to produce polypeptides with
variable length.
Levels of protein structure:
• 1- Primary structure.
• 2- Secondary structure.
• 3- Tertiary structure.
• 4- Quaternary structure.
Levels Of Protein Organization:
• Primary Structure - The sequence of amino acids
in the protein.
• Secondary Structure - The formation of a helixes
and b pleated sheets due to hydrogen bonding
between the peptide backbone.
• Tertiary Structure - Folding of helixes and sheets
influenced by R groups.
• Quaternary Structure - The association of more
than one polypeptide into a protein complex
influenced by R groups.
The primary structure of peptides and
proteins refers to the linear order.
The convention for the designation of the
order of amino acids is that the N-
terminal end is to the left (number 1
amino acid) and the C-terminal end is to
the right.
• Primary structure is stabilized by
peptide bonds and in some proteins
with disulfide bridges as well.
Cysteine is readily oxidized to form a covalently linked
dimeric amino acid called cystine, in which two cysteine
molecules or residues are joined by a disulfide bond The
disulfide-linked residues are strongly hydrophobic (non-
polar).
• The conformation of polypeptide
chain by twisting or folding is
referred to as secondary structure.
• The amino acids are located close to
each other in their sequence.
• The secondary structure is defined as the
relationship between the neighboring
amino acids in the polypeptide chain
which can be:
• 1- α-helix.
• 2- β-pleated sheets.
The α-helix is a common structure of proteins.
The formation of the α-helix is stabilized by
H-bonding between amide nitrogens and
carbonyl carbons of peptide bonds spaced four
residues apart.
Each turn of α-helix contains 4 amino acids.
• β-sheets are composed of 2 or more segments
of extended peptide chains.
• Segment at least consist of 5-10 amino acids.
• the hydrogen bonds are formed between the
neighboring segments of polypeptide chain.
• β-sheets are stabilized by H-bonding between
amide nitrogens and carbonyl carbons.
It refers to the three-dimensional structure of
the protein.
It is a compact structure with hydrophobic side
chains held interior while the hydrophilic
groups are on the surface of the protein.
It is stabilized by H-bonds, disulfide bonds and
ionic interactions (electrostatic bonds).
It is the relationship between different protein
subunits in a protein.
 The protein may be dimeric, trimeric, tetrameric….
oligomeric protein.
The monomeric subunits are held together by H-
bonds and ionic interactions.
Oligomeric proteins can be composed of
multiple identical polypeptide chains or
multiple distinct polypeptide chains.
Proteins with identical subunits are termed
homooligomers
Proteins containing several distinct polypeptide
chains are termed heterooligomers
Hemoglobin, contains two α and two β subunits
arranged with a quaternary structure in the form,
(α2 β2).

Hemoglobin is, therefore, a hetero-oligomeric


protein
Denaturation of proteins

• Loss of all structures of protein except the primary


structure.
• Break of all bonds except the peptide and disulfide
bonds.
• Loss of protein function.
• Denaturizing agents include the followings :
1. Acids. 2. Alkalis. 3. Temperature.
THANK
YOU
KH.E.O

KH.SH.O

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