Protein: From the Greek proteios – “ of first importance” Functions of Proteins

 Naturally occuring unbranched polymer in which the  Hemoglobin: Transport protein that carries O2 in the
monomer units are amino acids blood
 Proteins account for 15% of a cell’s overall mass.  Keratin: Fibruos protein in hair, skin, and nails.
 Unlike lipids and carbohydrates, proteins are not  Insulin:
stored, so they must be consumed daily. o Protein hormone synthesized in the
 Current recommended daily intake for adults is 0.8 pancreas
grams of protein per kg of body weight (more is o Controls blood glucose levels
needed for children).  Actin & Myosin: Proteins that control muscle
contractions
Classification based on function
 Ferritin: Protein that stores iron in the liver
 Catalytic proteins - Enzymes (Biochemical Catalyst,  Collagen:
helps speed up the biochemical process in the body) o Fibruos protein in connective tissue
o Found in tendons, bone, cartilage, and
 Defense proteins - immunoglobins or antibodies blood vessels
 Transport proteins – hemoglobin, lipoproteins (Helps Protein Classification by Shape
transfer chemicals in the body)
There are 100,000 different proteins in the human body.
 Messenger proteins – insulin, glucagon
 Fibruos proteins: insoluble in water and used for
 Contractile proteins – actin, myosin structural purposes (keratin & collagen)
 Structural proteins - collagen, α-keratin (e.g skin,  Globular proteins: more or less soluble in water and
hair) used for nonstructural purposes

 Transmembrane proteins – protein channels Amino Acids

 Storage proteins – myoglobin (stores oxygen so that  Are the building blocks of proteins
it is readily available)  Contain carboxylic acid and amino groups
 Are ionized in solution (soluble in water)
 Regulatory proteins – proteolytic enzymes, zymogens  They are ionic compounds (solids – high melting
points)
 Nutrient proteins – casein, ovalbumin (Where amino
 Contain a different side group (R) for each
acids come from)

 Buffer proteins – hemoglobin (if there are changes in

the blood the PH will adjust)

o Buffer is the chemical term where the

protein absorbs extra acidity so that the PH
is maintained.

o Blood PH – Ranges from 0 – 14

 Neutral is 7, If it is below 7.35 the

person is considered to be in
acidosis.

 Fluid balance proteins – albumin, globulin

 Amino acids are classified as:

 Nonpolar (Neutral) amino acids (hydrophobic) with Ionization and pH

hydrocarbon (alkyl or aromatic) sides chains.

 Polar (Neutral) amino acids (hydrophilic) with polar

or ionic side chains.

 Polar Acidic amino acids (hydrophilic) with acidic side

chains (-COOH).

 Polar Basic amino acids (hydrophilic) with –NH2 side

chains.

There are only 20 different amino acids in the proteins in

humans. They are called a – amino acids.

o Humans cannot synthesize 10 of these 20 amino

The net charge on an amino acid depends on the pH of the
acids
solution in which it is dissolved.
o These amino acids must be obtained from a diet
(on an almost daily basis)

Each amino acid has a fixed and constant pI.

Fischer Projections

All of the a-amino acids are chiral (except glycine)

Four different groups are attached to central carbon

Peptide Biologically Active Peptides

A dipeptide forms:  Enkephalins, pentapeptides made in the brain, act as

pain killers and sedatives by binding to pain
 When an amide links two amino acids (Peptide
receptors.
bond).
 Addictive drugs morphine and heroin bind to these
 −
Between the COO of one amino acid and the NH3 + same pain receptors, thus producing a similar
of the next amino acid. physiological response, though longer lasting.
 Enkephalins belong to the family of polypeptides
called endorphins (16-31 amino acids), which are
known for their pain reducing and mood enhancing
effects.

 Dipeptide: A molecule containing two amino acids

joined by a peptide bond.

 Tripeptide: A molecule containing three amino acids

joined by peptide bonds.

 Polypeptide: A macromolecule containing many

amino acids joined by peptide bonds.

 Protein: A biological macromolecule containing at

least 40 amino acids joined by peptide bonds.
 Oxytocin and vasopressin are cyclic nonapeptide
Naming of Peptides hormones, which have identical sequences except
for two amino acids.
 C-terminal amino acid: the amino acid at the end of
the chain having the free -COO- group (always
written at the right).
 N-terminal amino acid: the amino acid at the end of
the chain having the free -NH3+ group (always
written at the left).
o Begin from the N terminal.
o Drop “-ine” or “-ic acid” and it is replace by
“-yl”.
o Give the full name of amino acid at the C
terminal.

 Oxytocin stimulates the contraction of

uterine muscles, and signals for milk
production; it is often used to induce labor.

 Vasopressin, antidiuretic hormone (ADH)

targets the kidneys and helps to limit urine
production to keep body fluids up during
dehydration.
Conantokins are a small family of helical peptides that are Primary Structure of Proteins
derived from the venom of predatory marine snails of the
 The order of amino acids held together by peptide
genus Conus.
bonds.
 Each protein in our body has a unique sequence of
amino acids.
 The backbone of a protein.
 All bond angles are 120o, giving the protein a zigzag
arrangement.

 Conantokins are linear conopeptides 17–27 residues

in length that contain multiple γ-carboxyglutamate
residues in their sequence. Because of the lack of
disulfide bonds in the sequence of conantokins, the Cysteine
presence of Gla is important for the formation of a
The -SH (sulfhydryl) group of cysteine is easily oxidized to an -
helical structure. The binding of calcium ions to these
S-S- (disulfide).
peptides leads to a conformational change in their
structure thought to be important for their
bioactivity.104
 The therapeutic potential of clinically available
NMDA receptor antagonists is currently limited
because of the prevalence of undesirable side
effects, thought to be a result of a lack of specificity.
 Contulakin-G was discovered over 15 years ago as a
member of the neurotensin (NT) family from the
venom of predatory marine snail, Conus geographus
 Contulakin-G is a 16 amino acid peptide Primary Structure of Insulin

Dr. Lourdes J. Cruz is the National Scientist whose research  Is a hormone that regulates the glucose level in the
has contributed to the discovery of these peptides blood.
 Was the first amino acid order determined.
Structure of Proteins  Contains of two polypeptide chains linked by
disulfide bonds (formed by side chains (R)).
 Chain A has 21 amino acids and chain B has 30 amino
acids.
 Genetic engineers can produce it for treatment of
diabetes.
Secondary Structure of Proteins Secondary Structure Triple helix (Superhelix)

Describes the way the amino acids next to or near to each  Collagen is the most abundant protein.
other along the polypeptide are arranged in space.  Three polypeptide chains (three α-helix) woven
together.
 It is found in connective tissues: bone, teeth, blood
vessels, tendons, and cartilage.
 Consists of glycine (33%), proline (22%), alanine
(12%), and smaller amount of hydroxyproline and
hydroxylysine.
 High % of glycine allows the chains to lie close to
each other.
 We need vitamin C to form H-bonding (a special
enzyme).

Secondary Structure a-helix Tertiary Structure

 A section of polypeptide chain coils into a rigid spiral. The tertiary structure is determined by attractions and
repulsions between the side chains (R) of the amino acids in a
 Held by H bonds between the H of N-H group and polypeptide chain.
the O of C=O of the fourth amino acid down the
chain (next turn).

 looks like a coiled “telephone cord.”

 All R- groups point outward from the helix.

 Myosin in muscle and α-Keratin in hair have this

arrangement.

Secondary Structure B-pleated sheet

 Consists of polypeptide chains (strands) arranged

side by side.

 Has hydrogen bonds between the peptide chains.

 Has R groups above and below the sheet (vertical).

 Is typical of fibrous proteins such as silk.

Interactions between side chains of the amino acids fold a

protein into a specific three-dimensional shape.

(1)Disulfide (-S-S-)

(2) salt bridge (acid-base)

(3) Hydrophilic (polar)

(4) hydrophobic (nonpolar)

(5) Hydrogen bond

Tertiary Structure Quarternary Structure

 Occurs when two or more protein units (polypeptide

subunits) combine.

 Is stabilized by the same interactions found in

tertiary structures (between side chains).

 Hemoglobin consists of four polypeptide chains as

subunits.

 Is a globular protein and transports oxygen in blood

(four molecules of O2).

 CO is poisonous because it binds 200 times more

strongly to the Fe2+ than does O2 (Cells can die from
lack of O2).

Conjugated Proteins
Globular Proteins
They are composed of a protein unit and a nonprotein
 Have compact, spherical shape. molecule.

 Almost soluble in water.

 Carry out the work of the cells Synthesis, transport,

and metabolism.

Myoglobin

 Stores oxygen in muscles.

 153 amino acids in a single polypeptide chain (mostly
α-helix).

Fibruos Proteins
Sickle Cell Hemoglobin
 Have long, thin shape and insoluble in water.
 Sickle cell anemia is a disease where a single amino
 Involve in the structure of cells and tissues.
acid of both β subunits is changed from glutamic acid
 α-keratin: skin, nail, hair, and bone to valine.
 A genetic mutation in the DNA sequence that is
 β-keratin: feathers of birds responsible for synthesis of hemoglobin.
 Red blood cells containing these mutated
 α-keratin: hair, wool, skin, and nails
hemoglobin units become elongated and crescent
 They are made of two mainly α-helix chains coiled (sickle) shaped (more fragile).
around each other in a superhelix (supercoil).  These red blood cells will rupture capillaries, causing
pain and inflammation, leading to organ damage,
 These coils wind around other coils making larger and eventually a painful death.
and stronger structures (like hair).

 - α-helix chains bond together by disulfide bond (-S -

S-)

 - More disulfide bonds, more rigid materials (horns &

nails).
Summary of Protein Structure

Denaturation

 Is a process of destroying a protein by chemical and

physical means.
 We can destroy secondary, tertiary, or quaternary
structure but the primary structure is not affected.
 Denaturing agents: heat, acids and bases, organic
compounds, heavy metal ions, and mechanical
agitation.
 Some denaturations are reversible, while others
permanently damage the protein.
o Heat: H bonds, Hydrophobic interactions
o Detergents: H bonds
o Acids and bases: Salt bridges, H bonds.
o Reducing agents: Disulfide bonds
o Heavy metal ions (transition metal ions Pb2+,
Hg2+): Disulfide bonds
o Alcohols: H bonds, Hydrophilic interactions
o Agitation: H bonds, Hydrophobic interactions