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Levels of Protein Structure

1. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. 2. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves regular arrangements of amino acids like alpha helices and beta sheets. 3. Tertiary structure refers to the folding of polypeptide chains into compact three-dimensional structures. It is stabilized by interactions between amino acid side chains like disulfide bonds, hydrogen bonds, hydrophobic interactions, and ionic interactions.

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12 views

Levels of Protein Structure

1. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. 2. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves regular arrangements of amino acids like alpha helices and beta sheets. 3. Tertiary structure refers to the folding of polypeptide chains into compact three-dimensional structures. It is stabilized by interactions between amino acid side chains like disulfide bonds, hydrogen bonds, hydrophobic interactions, and ionic interactions.

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Divine Gaming
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Biochemistry topic

LEVELS OF PROTEINS
STRUCTURE
1. PRIMARY LEVEL OF PROTEIN STRUCTURE

• Definition;
• The sequence of amino acids in a protein is
called the primary structure of proteins
• It is important because many genetic diseases
are caused by abnormal amino acid sequences
PRIMARY LEVEL OF PROTEIN STRUCTURE

• In proteins, amino acids are linked together


covalently by PEPTIDE BONDS
• Therefore, the bonds which provide strength
to primary level are mainly PEPTIDE BONDS
PRIMARY LEVEL IS DETERMINED BY SEQUENCES
IN DNA (genetic code)

• The sequence of nucleotides in a protein-


coding region in DNA specifies the amino acid
sequence in a peptide
Genetic diseases are caused by mutations
in the DNA
• Any mutation in the DNA can cause a defect in the
amino acid sequence of a peptide (PRIMARY LEVEL IS
DEFECTIVE)
• For example; in sickle cell disease, there is
replacement of glutamate with valine, due to genetic
mutation
• Therefore sickle cell disease is a genetic disease
SECONDARY LEVEL OF PROTEIN
STRUCTURE

• Definition;

• The arrangements of amino acids in a protein


is called as secondary structure of proteins
• The polypeptides contain regular
arrangements of amino acids that are located
near each other
ARRANGEMENTS OF AMINO ACIDS IN
SECONDARY STRUCTURE

• These arrangements are:

1. α helix
2. β sheets
3. β bends (or β turns)
α- HELIX

• It is the most common arrangement


• It is rigid, right handed, spiral structure,
consisting of tightly packed, coiled
polypeptide backbone core, with the side
chains extending outwards
Hydrogen bonds provide strength to α
helix

• Helical structure is mainly stabilized by


hydrogen bonds between the peptide bond
3.6 amino acids per turn of helix

• Each turn of α helix, contains 3.6 amino acids


Amino acids that disrupt the α helix

• Proline amino acid inserts a kink in the chain,


interfering with the smooth, helical structure
Amino acids that disrupt the α helix

• Glycine amino acid also breaks helix because


of its R-group
β- SHEET

• It is an arrangement in which all the peptide


bond components are involved in hydrogen
bonding
• Because the surfaces of β sheets appear
‘pleated’ they are often called as ‘pleated
sheets’
Formation of β- sheet
• A β sheet is formed by two or more peptide
chains (β strands), aligned laterally and
stabilized by hydrogen bonds between the
carboxyl & amino groups of amino acids that are
either far apart in a single polypeptide (intra-
chain bonds) or are in different polypeptide
chains (inter-chain bonds)
3. β- BENDS

• β bends reverse the direction of a polypeptide


helping it to form a globular shape
• These are usually formed by 4 amino acids,
one of which is mostly proline (or glycine)
SUPER SECONDARY STRUCTURES
‘MOTIFS’

• Definition of MOTIFS;
• These are specific structural patterns in
proteins formed by combination of secondary
structural elements (α helix, β sheets & coils)
TERTIARY STRUCTURE OF PROTEINS
(folding of proteins)

• Tertiary structure refers to folding of domains


(subunits) and final arrangement of these
domains in the polypeptide
TERTIARY STRUCTURE OF PROTEINS
(folding of proteins)

• Tertiary structure is determined by the


primary structure of a polypeptide chain
DOMAINS:
• Domains are the functional & three
dimensional structural units of polypeptides
FORCES WHICH STABILIZE TERTIARY
STRUCTURE

• The three dimensional structure of each


polypeptide is determined by its amino acid
sequence
• Interactions among the amino acid side chains
guide the folding of the polypeptides to form a
compact structure
FORCES WHICH STABILIZE TERTIARY
STRUCTURE

1. Disulfide bonds:
• These covalent linkages are formed (-S-S-)
form the sulfhydryl groups between 2
cysteine amino acids
FORCES WHICH STABILIZE TERTIARY
STRUCTURE

2. Hydrophobic interactions:
• Amino acids with non-polar side chains tend
to be located in the interior of the
polypeptide molecule, where they associate
with other hydrophobic amino acids
FORCES WHICH STABILIZE TERTIARY
STRUCTURE

3. Hydrogen bonds:
• Amino acids side chains containing oxygen or
nitrogen-bound hydrogen which form
hydrogen bonds
FORCES WHICH STABILIZE TERTIARY
STRUCTURE

4. Ionic interactions:
• Negatively charged amino acids (glutamate,
aspartate) can interact with positively
charged groups (lysine, histidine, arginine)
PROTEIN FOLDING

• Interactions between the side chains of amino


acids determine how a linear polypeptide
chain folds into the three dimensional shape
of the functional protein

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