PROTEINS

Proteins
are
biochemicalcompoundscons
isting of one or more
polypeptidestypically folded
into
aglobularorfibrousform in
a biologically functional way.

History
Proteins were first described by theDutchchemistGerardus
Johannes Mulderand named by the Swedish chemistJns Jacob
Berzeliusin 1838. Early nutritional scientists such as the
GermanCarl von Voitbelieved that protein was the most
important nutrient for maintaining the structure of the body,
because it was generally believed that "flesh makes flesh. The
central role of proteins as enzymes in living organisms was
however not fully appreciated until 1926, whenJames B.
Sumnershowed that the enzymeureasewas in fact a
protein.The
first
protein
to
besequencedwasinsulin,
byFrederick Sanger, who won the Nobel Prize for this
achievement in 1958. The firstprotein structuresto be solved
werehemoglobinandmyoglobin, byMax PerutzandSir John
Cowdery Kendrew, respectively, in 1958.The three-dimensional
structures of both proteins were first determined byX-ray
diffraction analysis; Perutz and Kendrew shared the 1962Nobel
Prize in Chemistryfor these discoveries.

PROTEIN STRUCTURE

An-amino acid. The CH

atom is omitted in the
diagram.

Two amino acids

CO-R-N rule

Bond angles for and

Levels of Protein Structu

Primary Structure

Theprimary structurerefers to amino acid sequence of the

polypeptide chain. The primary structure is held together
bycovalentorpeptide bonds, which are made during the
process ofprotein biosynthesisor translation. The two ends
of thepolypeptide chainare referred to as the carboxyl
terminus(C-terminus)andtheaminoterminus(N-terminus)
based on the nature of the free group on each extremity.
Counting of residues always starts at the N-terminal end
(NH2-group),whichistheendwheretheaminogroupisnot
involvedinapeptidebond.

Secondary Structure
Secondary structurerefers to highly regular
localsub-structures.
These secondary structures are defined by
patterns ofhydrogen bondsbetween the
main-chain peptide groups. They have a
regular geometry, being constrained to
specificvaluesofthedihedralanglesand
on theRamachandran plot. Both the
alpha helix and the beta-sheet represent a
way of saturating all the hydrogen bond
donors and acceptors in the peptide
backbone.

Levels of Protein Structu

Tertiary Structure
Tertiary structurerefers to three-dimensional structure of a
single protein molecule. The alpha-helices and beta-sheets
are folded into a compact globule. The folding is driven by
thenon-specifichydrophobic interactions(the burial of
hydrophobicresiduesfromwater),butthestructureisstable
only when the parts of a protein domain are locked into
place byspecifictertiary interactions, such assalt bridges,
hydrogen bonds, and the tight packing of side chains and
disulfide bonds. The disulfide bonds are extremely rare in
cytosolic proteins, since the cytosol is generally a reducing
environment.

Quaternary Structure
Quaternary structure is a larger assembly of several
protein molecules or polypeptide chains, usually
calledsubunitsinthiscontext.Thequaternarystructureis
stabilized by the same non-covalent interactions
anddisulfidebondsasthetertiarystructure.Complexesof
twoormorepolypeptides(i.e.multiplesubunits)arecalled
multimers.

FUNCTIONS OF PROTEIN
Antibodies

Hormonal Proteins

are specialized proteins involved in defending

the body from antigens (foreign invaders). One
way antibodies destroy antigens is by
immobilizing them so that they can be
destroyed by white blood cells.

Contractile Protein
are responsible for movement. Examples
include actin and myosin. These proteins are
involved in muscle contraction and movement.

Enzymes

are messenger proteins which help to

coordinate certain bodily activities.
Examples include insulin, oxytocin,
and somatotropin. Insulin regulates
glucose metabolism by controlling the
blood-sugar concentration. Oxytocin
stimulates contractions in females
during childbirth. Somatotropin is a
growth hormone that stimulates
protein production in muscle cells.

Structural Proteins

are proteins that facilitate biochemical reactions.

They are often referred to as catalysts because
they speed up chemical reactions. Examples
include the enzymes lactase and pepsin. Lactase
breaks down the sugar lactose found in milk.
Pepsin is a digestive enzyme that works in the
stomach to break down proteins in food.

are fibrous and stringy and provide

support. Examples include keratin,
collagen,
and
elastin.
Keratins
strengthen protective coverings such
as hair, quills, feathers, horns, and
beaks. Collagens and elastin provide
support for connective tissues such as
tendons and ligaments.

FUNCTIONS OF PROTEIN
Storage Proteins
store amino acids. Examples include ovalbumin
and casein. Ovalbumin is found in egg whites
and casein is a milk-based protein.

Transport Proteins
are carrier proteins which move molecules from
one place to another around the body. Examples
include
hemoglobin
and
cytochromes.
Hemoglobin transports oxygen through the
blood. Cytochromes operate in the electron
transport chain as electron carrier proteins.

PROTEIN METABOLISM
Proteinmetabolismdenotes
the
variousbiochemicalprocesses
responsible
for
the
synthesis
ofproteinsandamino acids, and the
breakdown of proteins (and other large
molecules, too) bycatabolism.
Protein anabolism is the process by which protein are formed from amino
acids (aka anabolic amino acid synthesis).
Protein catabolism is the process by which proteins are broken down to
their amino acids. This is also calledproteolysis.

Proteins contain carbon, hydrogen, oxygen, nitrogen , and sometimes other

atoms. They form the cellular structural elements, are biochemical catalysts,
and are important regulators of gene expression . Nitrogen is essential to
the formation of twenty different amino acids, the building blocks of all body
cells. Amino acids are characterized by the presence of a terminal carboxyl
group and an amino group in the alpha position, and they are connected by
peptide bonds.
Digestion breaks protein down to amino acids. If amino acids are in excess
of the body's biological requirements, they are metabolized to glycogen or
fat and subsequently used for energy metabolism. If amino acids are to be
used for energy their carbon skeletons are converted to acetyl CoA, which
enters the Krebs cycle for oxidation, producing ATP. The final products of
protein catabolism include carbon dioxide, water, ATP, urea, and ammonia.
Vitamin B 6 is involved in the metabolism (especially catabolism) of amino
acids, as a cofactor in transamination reactions that transfer the nitrogen
from one keto acid (an acid containing a keto group [-CO-] in addition to
the acid group) to another. This is the last step in the synthesis of
nonessential amino acids and the first step in amino acid catabolism.
Transamination
converts
amino
acids
to
L-glutamate,
which
undergoes oxidative deamination to form ammonia, used for the synthesis
of urea. Urea is transferred through the blood to the kidneys and excreted
in the urine.

The glucose-alanine cycle is the main pathway by which amino groups from
muscle amino acids are transported to the liver for conversion to glucose.
The liver is the main site of catabolism for all essential amino acids, except
the branched-chain amino acids, which are catabolized mainly by muscle
and the kidneys. Plasma amino-acid levels are affected by dietary
carbohydrate through the action of insulin, which lowers plasma amino-acid
levels (particularly the branched-chain amino acids) by promoting their
entry into the muscle.
Body proteins are broken down when dietary supply of energy is inadequate
during illness or prolonged starvation. The proteins in the liver are utilized
in preference to those of other tissues such as the brain. The
gluconeogenesis pathway is present only in liver cells and in certain kidney
cells.

Disorders of amino acid metabolism include phenylketonuria , albinism,

alkaptonuria,
type
1
tyrosinaemia,
nonketotic
hyperglycinaemia,
histidinaemia, homocystinuria, and maple syrup urine disease.

S
N
I
E
T
O
R

S
I
S
E
H
T
YN

is
the
process
in
which cells build proteins. The term
is sometimes used to refer only to
protein translation but more often
it refers to a multi-step process,
beginning
with amino
acid
synthesis and transcription of nucle
ar DNA into messenger RNA, which
is then used as input to translation.

PROTEIN SYNTHESIS PRESENTATION

Protein Rich-Foods
Beans
As mentioned before, one half cup of
beans contains as much protein as a 3 oz
steak! Beans are a cheap, easy solution to
just about any meal. Try black beans in a
taco for lunch or a side of lima beans with
your dinner.

Eggs
One egg contains 6 grams of protein.
Eggs also contain many vital vitamins and
minerals and all of the essential amino
acids. An egg over-easy is a great
breakfast or try a poached egg with
spinach for dinner.

Dairy
Milk, cheese, and yogurt are all protein
rich foods. Milk contains about 6.3 grams
of high quality protein! Dairy products also
contain calcium, which is great for strong
bones and teeth. Add milk or yogurt to a
smoothie and have some cubes of cheddar
cheese as a snack- cheddar contains 25
grams of protein for every 100 grams.

Seafood
Seafood is a great way to get
healthy, high quality protein. Fishes
such as salmon contain Omega-3
Fatty Acids, which is great for the
heart and brain. Try salmon with
brown
rice
and
kale
for
an
extremely healthy, protein charged
dinner.

Protein Rich-Foods
Poultry
Lean white meats such as turkey or chicken
(without the skin) are high in protein low fat
foods. Either a turkey sandwich or a chicken salad
would be a perfect lunch to get you through the
rest of the day without being hungry.

Soy
Soy is a great form of protein for vegans or
vegetarians. Studies have shown that 25 grams
of soy protein can reduce the risk of heart
disease. Try edamame beans as a pre-dinner
snack or a glass of soy milk in the morning with
breakfast.

Beef
A lean cut of beef is an excellent source of
high quality protein. Beef contains about 25
grams of protein and has zinc, iron, and
vitamin B12. Try a lean cut of beef with crisp
iceberg salad or oven roasted potatoes.

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