Lecture#4

General Info about Proteins
Most diverse and

most important
macromolecules.
Our entire DNA
codes for the making
of proteins, and
nothing else.
Therefore they are
involved in
everything cells do.
Protein Structure
Proteins are polymers
of amino acids folded
into a specific 3D
shape that belays its
function.
Amino acids are made
up of a central carbon
atom connected to an
amino group, carboxyl
group, a hydrogen
atom and an R group
(side chain).
Amino Acids
Amino acids are considered to be amphiprotic
because they possess both an acidic terminus
(carboxyl group) and a basic terminus (amino
group).
Humans use 20 different amino acids, so there
are twenty different R-groups
Amino Acids
8 of these amino acids are known as essential
amino acids because our body cannot make
them from simpler substances, so we must get
these amino acids from our diet.
Amino Acids
Amino acids can be
classified based on
their R group in two
main ways:
i) polarity: polar
(water-soluble)
versus non-polar
(lipid soluble)
ii) electric charge:
acidic (negatively
charged) versus
basic (positively
charged)
Amino Acids
Linking Amino Acids to make a
Protein
All proteins have a
specific shape,
unique to that
protein. This final
shape is known as
the conformation of
the protein and it
depends entirely
upon the amino acid
sequence the protein
contains.
Protein
The joining of amino
acids together is
another example of a
dehydration synthesis
reaction. The linkage
between two amino
acids is known as a
peptide bond.
The growing
polypeptide chain will
always have an amino
terminus (A-terminus)
and a carboxyl
terminus (C-terminus).
Protein
All specific proteins
have the same exact
polypeptide sequence
(i.e. all insulin proteins
contain the exact same
polypeptide sequence),
which is determined
by DNA.
Structural proteins
are usually linear.
Functional proteins
form a globular shape.
Globular Proteins
Globular proteins
are composed of one
or more polypeptide
chains that have a
rounded, spherical
conformation.
Globular proteins
have four levels of
structure
Space filling and ribbon models of lysozyme, a protein
assembled from 129 amino acids.
• The primary structure of a protein is the
sequence of amino acids dictated by DNA.
met-enkephalin tyr-gly-gly-phe-met
leu-enkephalin tyr-gly-gly-phe-leu
oxytocin gly-leu-pro-cys-asn-gln-Ile-tyr-cys
vasopressin gly-arg-pro-cys-asn-gln-phe-tyr-cys
Sickle cell anemia is a disorder that is due to a
single amino acid substitution in the primary
structure of hemoglobin
Lysozyme
Coiling and folding of the
amino acid chain defines a
protein’s secondary structure.
This secondary structure is due
to hydrogen bonds between
adjacent portions of the
polypeptide chain.
Alpha-helix: coiled
appearance due to the
electronegative oxygen
from the carboxyl group
of one residue forming a
hydrogen bond with the
electropositive hydrogen
from the amino group of
another residue four
residues away.
Ex. Keratin, a protein in
hair, is almost
completely alpha-helical.
Stereo image of α-helix
Beta-pleated sheets: two
parts of the polypeptide
chain run parallel to one
another, hydrogen bonds
form in between, resulting
in a folded appearance.
Ex. Spider silk (a protein)
gets its strength from beta-
pleated sheets, and is the
basis for the whole Biosteel
industry.
The tertiary structure of the protein is based upon the
interactions between the R groups of amino acids.
a) interactions between the R groups of amino acids
and their environment.
Polar R groups will want to interact with water on
the outside of the polypeptide;
Non-polar R groups will want to move towards the
inside of the folds of the polypeptide.
Cytochrome c. Hydrophilic side chains are shown in green and are located mainly
on the surface of the protein where they come in contact with the aqueous
cytoplasm. Hydrophobic side chains are shown in red are primarily located within
the interior of the protein.
b) interactions between the R groups of different amino acids.
As shown in the diagram below, there are four main
interactions between R groups of different amino acids.
Stereo image of insulin
Stereo image of cytochrome c
The association of two or more polypeptide chains to
form a functional protein constitutes the quaternary
structure of a protein.
Collagen Hemoglobin

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General Info about Proteins

Most diverse and

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