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Greek Proteios - First

Proteins are essential biomolecules that perform many critical functions in living organisms. They are composed of amino acids linked together in a chain and have a hierarchical structure from primary to quaternary levels. The document discusses the classification, functions, and structures of proteins. It explains that proteins fold into secondary and tertiary structures defined by hydrogen bonding and other weak interactions between amino acid side chains. Mutations altering a protein's amino acid sequence can cause disease by changing its structure and function.

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54 views36 pages

Greek Proteios - First

Proteins are essential biomolecules that perform many critical functions in living organisms. They are composed of amino acids linked together in a chain and have a hierarchical structure from primary to quaternary levels. The document discusses the classification, functions, and structures of proteins. It explains that proteins fold into secondary and tertiary structures defined by hydrogen bonding and other weak interactions between amino acid side chains. Mutations altering a protein's amino acid sequence can cause disease by changing its structure and function.

Uploaded by

madhavanssn
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Greek proteios - first

Occurrence and Function


Plants & Animals ( including bacteria)
All type of organs : muscle, blood , bone etc
Catalyses reactions, provides immunity, responsible for structural
support, transports message , matter etc.,
In short everywhere and everything
Importance
Classification
Functions
Hierarchy of Structure
Test for Proteins
Classification of proteins
Based on Function
Enzymes: Accelerate biochemical reactions
(Proteases)
Structural: Form biological structures
(Bone , muscle)
Transport: Carry biochemically important substances
(hemoglobin)
Defense /Immunity: Protect the body from foreign invaders
(Antibodies)
Based on Structure
Globular: Example Complex folds, irregularly shaped
tertiary structures
Fibrous: Extended, simple folds -- generally
structural proteins
Occurrence in Cell
Membrane: In direct physical contact with a membrane;
(generally water insoluble)
Based on Amino Acids
Based on Amino Acids
7
Incomplete protein Incomplete protein
Lack one of more of Lack one of more of
the essential amino the essential amino
acids acids
Most vegetable Most vegetable
proteins are proteins are
incomplete proteins incomplete proteins
Beans are an Beans are an
exception to this exception to this
generalizations generalizations
Amino acids are the building blocks of proteins. Amino acids are the building blocks of proteins.
Proteins are natural polymers of successive amino Proteins are natural polymers of successive amino
acids acids
There are 20 different amino acids that make up There are 20 different amino acids that make up
human proteins human proteins
Polymerisation / Peptide formation
When two amino acids combine, there is a
formation of an amide and a loss of a water
molecule
By convention, N-terminal amino acid on left and C-terminal amino
acid on right
Two Amino Acids are connected by one
PEPTIDE BOND
n=1-10 peptide ( 2 -11 residues)
n>10<100 polypeptide (>11 to <101)
n=>100 protein (>101 residues / mol.wt
10000)
Hierarchical nature of protein structure
Hierarchical nature of protein structure
Primary structure (Amino acid sequence)

Secondary structure -helix, -sheet

Tertiary structure Three-dimensional structure


formed by assembly of secondary structures

Quaternary structure Structure formed by more


than one polypeptide chains
Protein Structure
Protein Structure
Hierarchy of protein structure Hierarchy of protein structure
Protein Structure
Protein Structure
-
-
Primary
Primary
Protein: chain of amino acids joined
by peptide bonds
Amino Acid
Central carbon (C

) attached to:
Hydrogen (H)
Amino group (-NH
2
)
Carboxyl group (-COOH)
Side chain (R)
Peptide Chain
Peptide Chain
-carboxyl of one amino acid is joined to -amino of a second
amino acid (with removal of water)
only -carboxyl and -amino groups are used, not R-group
carboxyl or amino groups
40% double bond character (Caused by resonance)
The peptide bond is planar and rigid
Importance of sequencing
Importance of sequencing
Linear sequence of amino acids forms primary
structure
Sequence essential for proper physiological
function
Sequence similarity implies structural, functional,
and evolutionary commonality
Any change in a particular sequence can cause
deadly disease
Sickle Cell anemia
Replacement of single glutamine with valine in just one
polypeptide chain of hemoglobin (Hb) alters its structure and
function
Sickle
Sickle
-
-
cell
cell
Rigid structure of sickle cells blocks capillaries
and prevents red blood cells from delivering
oxygen
Capillary Blockage
Capillary Blockage
21
Secondary Structure
Secondary Structure
The chemical nature of the carboxyl and amino groups of
all amino acids permit hydrogen bond formation (stability)
and hence defines secondary structures within the
protein.
The R group has an impact on the formation of secondary
structures
This leads to a propensity for amino acids to exist in a
particular secondary structure conformation
Helices and sheets are the regular secondary structures,
but irregular secondary structures exist and can be critical
for biological function
In order to carry out their function (for instance as
enzymes or antibodies), proteins must take on a
particular shape, also known as a "fold." Thus, proteins
are truly amazing machines: before they do their work,
they assemble themselves! This self-assembly is called
"folding.
Protein folding is FAST!!
Typically a couple of seconds some within millionth of a
second ( in micro seconds)
Folding is CONSISTENT!!
Involves weak forces Non-Covalent
Hydrogen Bonding, van der Waals,Salt Bridges
Folding results in
- helix
- pleated sheet
Random coil
Hydrogen Bonding
And Secondary Structure
alpha-helix
beta-sheet
Two common secondary structures are
the Helix
(1-4 H bonding)
and the sheet
Parallel C terminal on both chains
Anti parallel C on one and N on other
25
C
C
C
N
26
Alpha Helix
Alpha Helix
It is the result of
intra chain
hydrogen bonding
A helix can turn
right or left from N
to C terminus only
right-handed are
observed in nature
27
Alpha Helix Continued
Alpha Helix Continued
There are 3.6
residues per turn
Helices in
proteins are right
handed.
R groups
directed outward
from coil
28
Beta Sheets
Beta Sheets
29
Beta Sheets Continued
Beta Sheets Continued
Anti parallel beta sheet is more common
Mixed sheets are less common
-sheets are almost never flat
One -sheet wraps around another leading to a barrel shape
(a beta barrel)
Secondary Structure
Beta bulge is a variant; residue on one
strand forms two hydrogen bonds with
residue on other causes one strand
to bulge occurs most frequently in
parallel sheets
Random coil
Random coil
random structure, just
non-repeating
Random coil has fixed
structure within a given
protein
Commonly called
connecting loop region
Structure determined by
bonding of side chains
(i.e. not necessarily
hydrogen bonds)
32
Tertiary Structure
Tertiary Structure
Myoglobin (Kendrew 1958) and hemoglobin
(Perutz 1960) gave us the proven
experimental insights into tertiary structure
as secondary structures interacting by a
variety of mechanisms
While backbone interactions define most of
the secondary structure interactions, it is
the side chains that define the tertiary
interactions
Tertiary Structure
Structure Stabilizing Interactions
Structure Stabilizing Interactions
Noncovalent
Van der Waals forces (transient, weak
electrical attraction of one atom for
another)
Hydrophobic (clustering of nonpolar
groups)
Hydrogen bonding
Disulfide Bonds & Disulfide Bridge
Disulfide Bonds & Disulfide Bridge
Side chain of cysteine (1) contains highly reactive
thiol group
Two thiol groups form a disulfide bond (2)
1 2
Disulfide Bridge
Disulfide Bridge

Linking Distant Amino Acids


Linking Distant Amino Acids
Protein: The Machinery of Life
Protein: The Machinery of Life
Life is the mode of existence of proteins, and this
mode of existence essentially consists in the
constant self-renewal of the chemical
constituents of these substances.
Friedrich Engles, 1878
NH
2
-Val-His-Leu-Thr-Pro-Glu-Glu-
Lys-Ser-Ala-Val-Thr-Ala-Leu-Trp-
Gly-Lys-Val-Asn-Val-Asp-Glu-Val-
Gly-Gly-Glu-..

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