PROTEINS

protein

is naturally-occurring, unbranched polymer in which the monomer units are amino acids.

Protein are most abundant molecules in the cells after water-account for about 15% of a cell's overall mass.

proteins

have the widest array of functions.

keratin and collagen

for example, form long insoluble fibers, giving strength and support to tissues. Hair, norns, hooves,

fingernails are all made up of

keratin

collagen

is found in bone, connective tissue, tendons, and cartilage.

membrane proteins

transport small organic molecules and ions across cell membranes.

insulin

the hormone that regulates blood glucose levels,

hemoglobin

which transports oxygen from the lungs to tissues, are proteins.

enzymes

are proteins that catalyze and regulate all aspects of cellular function.

hemoglobin

transport protein that careies O2 in the blood

collagen

fibrous protein in connective tissue

collagen

found in tendons,bone,cartillage and blood vessels

ferritin

protein that stores iron in the liver

Actin and myosin

Proteins that control muscle contractions

Keratin

Fibrous protein in hair skin nails

Myoglobin

Protein that stores 02 in tissues

Insulin

Protein hormone synthesized in the pancreas / controls blood glucose levels

Biomolecules that contain many amide bonds formed by joining amino acids together

proteins

Protein

Comes from the Greek proteios meaning “of first importance”

1.1 g/ kg

Children 1-3 years

0.95 g/kg

Children 4-13 years

0.85 g/kg

Children 14 - 18 years

0.8 g/kg

Adults

Albuminoids

Keratin in skin, hair, nails, collagen in cartilage

Albumins

Egg albumin , serum albumIn

Globulins

Antibodies

Histones

Chromatin in chromosomes

Conjugated (complex) protein

A protein that has one or more non- amino acids entities ( prosthetic group )

Can be organic or organic

Prosthetic group

Hemoproteins

Carrier of o2 in blood oxygen binder in muscles

Lipoproteins

Lipid carrier

Glycoproteins

Antibody/ lubricant in mucous secretions antiviral protection

Phosphoproteins

Enzyme in glycogen phosphorylation

Nucleoproteins

Site for protein synthesis in cells / self-replicating , infectious complex

Metalloproteins

Storage complex for iron enzyme in alcohol oxidation

Keratins, found in

Wools ) hooves ) silk and fingernails

Collagens found in

Tendons, bone and other connective tissue

Found in blood vessels and ligaments

Elastins

Myosin's

Found in muscle tissue

Fibrin

Found in blood clots

Fibrous proteins (insoluble)

Keratin collagens elastins myosin's fibrin

Globular proteins (soluble)

Insulin myoglobin hemoglobin transferrin immunoglobulin)

Regulatory hormone for controlling glucose metabolism

Insulin

Oxygen storage in muscles

Myoglobin

Iron transport of in blood

Transferrin

Immunoglobulins

Involved in immune system responses

Catalytic proteins

Enzymes are best known for their catalytic role ) almost every chemical reaction in the body is driven by an enzyme

Defense proteins

Immunoglobulins or antibodies are central tofunctioning of the body's immune system

Transport proteins

Bind small biomolecules e.g. Oxygen and other ligands. and transport them to other locations in the body andrelease them on demand

Messenger proteins

Transmit signals to coordinate biochemical processesbetween different cells, tissues and organs.

Insulin and glucagon

Regulate carbohydrate metabolism

Human growth hormone

Regulate body growth

Necessary for all forms of movement

Contractile proteins

Actin and myosin

Muscles contain filament like contractile proteins

Structural proteins

Confer stiffness and rigidity

Component of cartilage

Collagen

Keratin

Gives mechanical strength as well as protective covering to hair )

Fingernails I feathers I hooves

Transmembrane proteins

span a cell membrae and help control the movement of small molecules and ions.

transmembrane proteins

have channels - help molecules to enter and exist the cell

transmembrane proteins

transport is very selective - allow passage of one type of molecule or ion

storage proteins

bind and store small molecules

ferritin

an iron storage proteins - saves iron for usse in the biosynthesis of new hemoglobin molecules

myoglobin

an oxygen-storage protein present in muscle

often found ‘embeddded’ in the exterior surface of cell membranes- act as sites for receptor molecules

regulatory proteins

nutrient proteins

prticularly important in the early stages of life- from embryo to infant

enzymes

proteins with the role of biochemical catalyst are called enzymes

amino group (NH2) and carboxyl group (COOH)

the 2 functional groups that contain amino acids

20 amino acids

number of amino acids that occur naturally in proteins

glycine

simplest amino acid and has R=H

ACIDIC AMINO ACIDS

AMINO ACIDS WITH ADDITIONAAL COOH GROUP IN THE SIDE CHAIN

BASIC AMINO ACIDS

THOSE WITH AN ADDITIONAL BASIC N ATOM IN THE SIDE CHAIN

NEUTRAL AMINO ACIDS

ALL OTHERS AMINO ACIDS

ZWITTERION

PROTON TRANSFER FROM THE ACID TO THE BASE FORMS A SALT

10 ESSENTIAL AMINO ACIDS

HUMANS CAN ONLY SYNTHESIZE THAT NEEDED FOR PROTEINS

ESSENTIAL AMIO ACIDS

amino acids that must be obtained by foods

non essential amino acids

amino acids that can be created by body

ammonium cation

amino group bears a net positive charge

carboxylate anion

carboxyl group bears a net negatie charge

isoelectric point

the pH at which the amino acids exists primarily in its neutral form

peptides and proteins

amino acids are joined together by amide bonds, they form larger molecules called——-

dipetide

has two amino acids joined together by one amide bond

tripetide

has tree amino acids joined together by two amide bonds

polyeptides and proteins

both have many amino acids joined together in long linear chains, but the term protein is usually reserved for polymeea of more than 40 amino acids

peptide bonds

amide bonds in peptides

acid residues

the individual amino acids

N-terminal

the amino acid with the free -NH3+ group on the ą carbon

C- terminal

the amink acid with the free -COO- group on the a carbon

primary, secondary, tertiary and quaternary structure

four levels of structure

primary structure

particular sequence of amino acids that is joined together by peptide bonds

amide bond

a primary structure that joins the amino acids

trigonal planar

a carbonyl carbon of the amide has —- geometry