Starting With the Gracious Name

of ALLAH Almighty
 Group e (NEWTON AND
FUNCTION OF PROTEINS)

Group Members:-
Abubakar Hafeez
Eisha Rana
Mahnoor Sajjad
Noman Akram
Saad Ahsan Khan
Newton
His name was ISSAC NEWTON
Lived from dec 25th,1642 to march 20th,1727
Was an english scientist , mathematician and
natural philosopher
In his time he played a vital role in the scientific
resolution helping to advance the fields of
physics , astronomy , mathemtics and natural
science
 From this he estabilished a ligacy that would
dominate thee science for the next three
centuries
because of his extensive contribution he was
regarded as one of the most influential scholars
in the history of science
Achievements

He discovered the THREE LAWS OF

MOTION which was his biggest
achievement.
He also formulated the law of universal
gravitation in the PRINCIPIA
F=Gm1m2/r2
He also predicted that the earth was
likely shaped as an OBLATE Spheroid
i.e ., sphere that experienced flattening
at the poles
 In 1666 , he began contributing
to the fields of optics
From 1670 to 1672 he lectured
at the university of cambridge
He also studied speed of sound
STRUCTURE OF PROTEINS

Proteins are polymers of amino acids

covalently linked through peptide bonds
into a chain.Withinandoutsideofcells,
proteinsserveamyriadoffunctions,including
structuralroles(cytoskeleton),ascatalysts
(enzymes),transportertoferryionsand
moleculesacrossmembranes,andhormones
tonamejustafew.
 With few exceptions, biotechnology
is about understanding, modifying
and ultimately exploiting proteins
for new and useful purposes.To
accomplish these goals, one would like
to have a firm grasp of protein structure
and how structure relates to function.
This goal is, of course, much easier to
articulate than to realize! The objective
of this brief review is to summarize only
the fundamental concepts of protein
structure.
Shape = Amino Acid
Sequence
Proteins are made of 20 amino acids
linked by peptide bonds
Polypeptide backbone is the
repeating sequence of the N-C-C-N-
C-C in the peptide bond
The side chain or R group is not part
of the backbone or the peptide bond
Polypeptide Backbone
Amino Acids
Levels Of Organizations:

Primary structure
Amino acid sequence of the protein
Secondary structure
H bonds in the peptide chain backbone
-helix and -sheets
Tertiary structure
Non-covalent interactions between the R
groups within the protein
Quaternary structure
Interaction between 2 polypeptide chains
Primary Structure
The primary structure of protein
refers to the linear sequence of
amino acids in polypeptide chains
The primary structure is held
together by covalent bonds which
are made by process of protein
synthesis
Secondary Structure
Within the long protein chains there
are regions in which the chains are
organized into the regular structures
knows as helix and pleated
sheets
These are the secondary structures
in proteins held together by H-
bonding
 Helix
Formed by a H-bond
between every 4th peptide
bond C=O to N-H
Usually in proteins that
span a membrane
The helix can either coil
to the right or the left
Can also coil around each
other coiled-coil shape
a framework for structural
proteins such as nails and
skin
-pleated sheets
Core of many proteins is
the sheet
Form rigid structures with
the H-bond
Can be of 2 types
Anti-parallel run in an
opposite direction of its
neighbor (A)
Parallel run in the same
direction with longer
looping sections between
them (B)
Tertiary Structure
It is a three
dimensional
structure of protein
It will have a single
polypeptide chain
backbone with one
or more protein
secondary structures
, the protein domains
Amino acid side
chains may interact
and bond in no of
ways
Quaternary Structure
It involves the
clustering of several
individual peptide or
protein chains into a
final specific shape
A variety of bonding
interactions including
H-bonding , Salt
Bridges and disulfide
bonds hold the
various chains into
particular geometries
Domains

A domain is a basic structural unit of

a protein structure distinct from
those that make up the
conformations
Part of protein that can fold into a
stable structure independently
Different domains can impart
different functions to proteins
Proteins can have one to many
domains depending on protein size
Domains
Motifs
ItIs an amino acid
sequence pattern
found in proteins
They donot allow
us to predict the
biological functions
They are found in
proteins and
enzymes with
dissimilar functions
Protein Foldings
2 regular folding
patterns have been
identified formed
between the bonds of
the peptide backbone
-helix protein turns
like a spiral fibrous
proteins (hair, nails,
horns)
-sheet protein folds
back on itself as in a
ribbon globular protein
Protein Folding

The peptide bond allows for rotation

around it and therefore the protein
can fold and orient the R groups in
favorable positions
Weak non-covalent interactions will
hold the protein in its functional
shape these are weak and will take
many to hold the shape
Useful Proteins

There are thousands and thousands of

different combinations of amino acids
that can make up proteins and that would
increase if each one had multiple shapes
Proteins usually have only one useful
conformation because otherwise it would
not be efficient use of the energy
available to the system
Natural selection has eliminated proteins
that do not perform a specific function in
the cell
General Classifications Of
Proteins
Fibrous Protein :
It exists as long fibers that are usually
tough and insoluable in water i.e.,
Collagen and Keratin
Globular Proteins :
These are spherical , highly folded ,
and usually soluable in water i.e .,
enzymes , antibodies
Protein Families

Have similarities in amino acid

sequence and 3-D structure
Have similar functions such as
breakdown proteins but do it
differently
Single Subunit Protein
Multiple Subunit Protein
Hemoglobin
2 globin
subunits
2 globin
subunits
Conclusion
Any Questions ????
 Thanks
Have a nice day