Amino acids, Polypeptides and Proteins subtitle style Click to edit Master

4/14/12

Proteins
Derived from the Greek word proteios, which

means holding first place or first importance

Are instrumental in about everything that an

organism does

4/14/12

Proteins
are organic compounds composed

mainly of carbon, hydrogen, oxygen, and nitrogen

4/14/12

Functions
Structure Catalysis Movement Transport Hormones Protection Storage Regulation 4/14/12

Functions
Proteins are the overwhelming enzymes in

a cell and regulate metabolism by selectively accelerating chemical reactions.

4/14/12

Function - structure
Proteins are the main structural materials

for animals

4/14/12

 Chief constituents of skin, bones,

hair, and nails

Two important structural proteins

collagen and keratin

4/14/12

Collagen
Collagen is a type of protein. Fibrous in nature, it connects and supports

other bodily tissues, such as bone,tendons, muscles, andcartilage.

skin,

It also supports the internal organs and is

even present in teeth. There are more than 25 types of collagens that naturally occur in the body.

4/14/12

4/14/12

Keratin
Keratinis an extremely strong protein which

is a major component in skin, hair, nails, hooves, horns, and teeth.

The amino acidswhich combine to

formkeratinhave several unique properties, and depending on the levels of the various amino acids,keratincan be inflexible and hard, like hooves, or soft, as is the case with skin.

4/14/12

Keratin
Most of thekeratinthat people interact with

is actually dead; hair, skin, and nails are all formed from dead cells which the body sheds as new cells push up from underneath. If the dead cells are kept in good condition, they will serve as an insulating layer to protect the delicate newkeratinbelow them.

4/14/12

Keratin Structure

4/14/12

Function - catalysis
Virtually all reactions in living organisms are

catalyzed by proteins called enzymes. not used.

Very slow reaction will happen if enzymes are

4/14/12

Function - movement
Muscle expansion and contraction are

involved in every movement we make.

Muscles are made up of protein molecules

called myosin and actin.

4/14/12

4/14/12

Function - transport
A large number of proteins perform

transportation duties.
Hemoglobin protein in the blood

carries oxygen from lungs to the cells and carbon dioxide from cells to the lungs.

4/14/12

4/14/12

Function - hormones
Many hormones are proteins, including

insulin, erythropoietin, and human growth hormone.

4/14/12

Function - protection
When a protein from outside source or

other foreign substance antigen enters the body, the body makes its own proteins antibodies to counteract the foreign protein.
Blood clotting is another protective

function carried out by a protein fibrinogen without blood clotting, we will bleed to death from any small wound.

4/14/12

4/14/12

Function - storage
Some proteins store materials in the way

that starch and glycogen store energy.

Casein in milk and ovalbumin in eggs

store nutrients for newborn mammals and birds.

Ferritin a protein in the liver stores

iron.

4/14/12

Function - regulation
Some

proteins not only control the expression of genes thereby regulating the kind of proteins synthesized in a particular cell, but also dictate when such manufacture takes place.

4/14/12

Function
These are not the only functions of

proteins, but they are among the most important.

Any individual needs a great many

proteins to carry out these varied functions.

A typical cell contains about 9,000

different proteins; the entire human body has about 100,000 different proteins.

4/14/12

Major types
Fibrous proteins
Insoluble in water Used mainly for structural purposes

Globular proteins
More or less soluble in water Used mainly for nonstructural
4/14/12

purposes

Some common fibrous and Globular Proteins Name Fibrous Proteins ( insoluble) Collagens Elastins Fibrinogen Keratin
4/14/12

Occurrence and Use

Animal hide, tendons, connective tissues Blood vessels, ligament Necessary for blood clotting Skin, wool, feathers etc.

Some common fibrous and Globular Proteins Name Globular Proteins (soluble) Hemoglobin Immunoglobulin Insulin Occurrence and Use

4/14/12

Ribonuclease

Involve in oxygen transport Involve in immune response Hormone for controlling glucose metabolsim Enzymes controlling RNA synthesis

Structure-function connection

Humans have ten thousands of

different proteins, each with their own structure and function.

Proteins are the most structurally

complex molecules known.

Protein polymers are constructed

from the same set 0f 20 monomers, called amino acids.

4/14/12

Amino acids
An organic compound containing an

amino group and a carboxyl group

Can be synthesized in the laboratory Nature is more restrictive and uses

20 common amino acids to make up proteins.

4/14/12

Amino acids
The sequence of amino acids

determines a proteins shape and function.

The 20 common amino acids found

in proteins are called alpha amino acids.

Amino acid in which the amino

group is linked to the carbon atom next to the COOH carbon. 4/14/12

Amino acids
12 amino acids are made in the

human body.
Humans need to consume the

other 8 amino acids from sources such as nuts, beans, or meat

4/14/12

Classification of proteins
Simple Proteins
yield only amino acids when hydrolyzed

Conjugated Proteins
yield amino acids and one or more

additional products

4/14/12

Some Conjugated Proteins

Name Glycoproteins Composition Proteins bonded to a cabohydrates; e.g. Cell membrane Proteins bonded to fats and oils ( lipid); e.g. cholesterol Proteins bonded to a metal ion; e.g cytochrome ( biological energy)

Lipoprotein

Metalloproteins

4/14/12

Some Conjugated Proteins

Name Nucleoproteins Composition Proteins bonded to RNA Proteins bonded to a phosphate group; milk casein

Phosphoproteins

4/14/12

Classification according to polarity

Nonpolar
hydrophobic

Polar but neutral

hydrophilic

Acidic
hydrophilic

Basic
4/14/12

Hydrophilic

Amino acids
Several amino acids found in

proteins also serve functions distinct from the formation of peptides and proteins.
Histidine converted to histamine,

which causes stomach lining to secrete HCl and is associated with tissue inflammations and colds.
4/14/12

Amino acids
Tyrosine converted to dopamine

(neurotransmitter), epinephrine (adrenalin) and thyroxine

Glycine and glutamic acid

chemical messengers between nerve cells

4/14/12

Essential amino acids

Arginine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine
4/14/12 Tryptophan

Alanine

Non essential amino acids

Asparagine Aspartate Cysteine Glutamate Glutamine Glycine Proline Serine 4/14/12

Amino acids
Amino acid units in a given protein are

arranged in a definite sequence

The sequence of amino acids establishes

the proteins function.

Missing or misplaced amino acids may

alter the proteins biological function.

4/14/12

amphoterism
Amphoteric can act either as an

acid or as a base
The alpha-COOH and alpha-NH2

groups in amino acids are capable of ionizing (as are the acidic and basic R-groups of the amino acids).
4/14/12

Zwitterion (di-ion)
Amino acid with no ionizable R-group

and is electrically neutral

4/14/12

Formation of polypeptides

Proteins and peptides are polymers

of amino acids linked by peptide bonds

Also called amide bonds or

peptide linkage

4/14/12

Formation of polypeptides

Amide bonds results from the

condensation of an amino and a carboxyl group, releasing water

The amide group is polar, with

resonance giving partial double bond characteristics.

This helps peptides be soluble even

though the charges are lost during condensation. 4/14/12

Formation of polypeptides

Amino acids are joined together

when a dehydration reaction removes a hydroxyl group from the carbonyl end of one amino acid and a hydrogen from the amino group of another.
The resulting covalent bond is

called a peptide bond.

4/14/12

Formation of polypeptides

Repeating the process over and over

creates a long polypeptide chain.

At one end is an amino acid with a free

amino group the N-terminus and at the other is an amino acid with a free carboxyl group the C-terminus.

4/14/12

Formation of polypeptides
R groups.

The repeated sequence (N-C-C) is the

polypeptide backbone.
Attached to the backbone are the various Polypeptides range in size from a few

monomers to thousands.

4/14/12

Formation of polypeptides
general designation

Each amino acid is called a residue. The number of amino acids is reflected in a
2 amino acids dipeptide 3 amino acids tripeptide Several amino acids oligopeptides Many amino acids protein or

polypeptides

4/14/12

4/14/12

TRIPEPTIDE

4/14/12

Conformation
A proteinss function depends on its

specific conformation.
A functional proteins consists of one or

more polypetides that have been precisely twisted, folded, and coiled into a unique shape.
It is the order of amino acids that

determines what three-dimensional conformation will be.

4/14/12

Conformation
In almost every case, the function depends

on its ability to recognize and bind to some other molecule.

Antibodies bind to a particular foreign

substances that fir their binding sites. substrates, facilitating a chemical reaction. cell to another by binding to

Enzyme recognize and bind to specific

one 4/14/12

Neurotransmitters pass signals from

conformation
The folding of a protein from a chain of

amino acids occurs spontaneously.

The function of protein is an emergent

property resulting from its specific molecular order.

4/14/12

conformation
Three levels of structure: primary,

secondary and tertiary structure, are used to organize the folding within a single polypeptide.
Quarternary structure arises when two

or more polypeptides join to form a protein.

4/14/12

Primary structure
The primary structure of a protein is its

unique sequence of amino acids.

Lysozyme, an enzyme that attacks

bacteria, consists on a polypeptide chain of 129 amino acids.

The precise structure of a protein is

determined by inherited genetic information.

4/14/12

Primary structure
Even a slight change in primary structure

can affect a proteins conformation and ability to function.

In individuals with sickle cell disease,

abnormal hemoglobins, oxygen-carrying proteins, develop because of a single amino acid substitution.
These abnormal hemoglobins crystallize,

4/14/12

deforming the red blood cells and leading to clogs in tiny blood vessels.

Secondary structure
The secondary structure of a protein

results from hydrogen bonds at regular intervals along the polypeptide backbone.
Typical shapes that develop from

secondary structure are coils (an alpha helix) or folds (beta pleated sheets)

4/14/12

Secondary structure
The structural properties of silk are due to

beta pleated sheets.

The presence of so many hydrogen bonds

makes each silk fiber stronger that steel.

4/14/12

Tertiary structure
Tertiary structure is determined by a

variety of interactions among R groups and between R groups and the polypeptide backbone. among polar and/or charged areas, ionic bonds between charged R groups, and hydrophobic interactions and van der Waals interactions among hydrophobic R groups.

These interactions include hydrogen bonds

4/14/12

Tertiary structure
While these interactions are relatively weak,

disulfide bridges, strong covalent bonds that form between the sulfhydryl groups (SH) of cysteine monomers, stabilize the structure.

4/14/12

Quarternary structure
Quarternary structure results from the

aggregation of two or more polypeptide sub units. polypeptides that are supercoiled like a rope.
This provides the structural strength of their role

Collagen a fibrous protein of three

in connective tissue.

Hemoglobin is a globular protein with two

copies of two kinds of polypeptides.

4/14/12

conformation
A proteins conformation can change in

response to the physical and chemical conditions temperature, or other factors can unravel or denature a protein.

Alterations in pH, salt concentration,

These forces disrupt the hydrogen bonds, ionic

bond, and disulfide bridges that maintain the proteins shape

4/14/12

conformation
Some proteins can return to their

functional shape after denaturation, but other cannot, especially in the crowded environment of the cell.

4/14/12

conformation
In spite of the knowledge of the three-

dimensional shapes of over 10,000 proteins, it is still difficult to predict the conformation of a protein from its primary structure alone.
Most proteins appear to undergo

several intermediate stages before reaching their mature configuration.

4/14/12

conformation
The folding of many proteins is protected

by chaperonin proteins that shield out bad influences.

4/14/12