Proteins

By Sulaiman D. Tahsin

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1. Introduction 2. General structure 4 categories of protein structure 3. Functions 4. Properties physical properties chemical properties 5. Classification 6. Detect the presence of protein 7. Amino acids general structure classifications physical properties chemical properties 8. Nutritional properties

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Introduction
Comes from the word proteios preeminence Organic compounds of high molecular weight, made up of a-amino acid joined by peptide linkage The presence of nitrogen distinguishes protein from carbohydrates and fats. Proteins contains an average of 16% nitrogen.

 5,000 to 8,000,000 molecular weight

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General Structure
C, H, O, N and with few exceptions, sulfur. Most proteins also contain phosphorus and specialized protein contains very small amounts of iron, copper, and other inorganic elements. Polymers of amino acids joined by peptide linkage

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Theory of peptide linkage the most satisfactory Link between (-NH2) and (-COOH)

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4 categories of protein structure

Primary structure number and sequence of amino acid polypeptide chain
By convention, it begins with a.a. whose amino group is free ( N-terminal end) and ends with carboxyl group (C-terminal end)

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Secondary structure
Shape (conformation) of molecule a-helix coiled spring maintained by intramolecular H-bonds b-pleated sheath maintained by intermolecular Hbonds

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Tertiary structure
Specific folding and bending - side chain is responsible (R group) H-bonding, Salt bridges, disulfide bridge, hydrophobic interaction responsible for stability 2 major groups : fibrous and globular

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Fibrous parallel fashion along an axis, to yield long sheets or fibers. - insoluble in water and dilute salt solution - basic structural unit in connective tissues such as collagen and tendons and bone matrix
Globular protein compact spherical or globular shape - soluble in aqueous solution - hemoglobin, serum albumin Some are in between like myosin and fibrinogen

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Quaternary structure
Determines how the different subunits organized as a whole

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Biological function is based upon its conformation. Any change in its conformation may lead to loss of biological activity mild change in physical condition change in temperature change in pH presence of detergents

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Function
Structural function catalysis of biochemical reactions regulation of metabolic processes defense against infection( antibodies) Acid-base balance Transport Energy source transmission of heredity characteristics muscular activity (contraction)

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Structural Functions: Collagen is the most abundant protein in mammals, and gives bone and skin their strength Keratin provides structure to hair and nails
Elastin is a protein in connective tissue that is elastic and allows many tissues in the body to resume their shape after stretching or contracting. Elastin helps skin to return to its original position when it is poked or pinched

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catalysis of biochemical reactions

ENZYMES Enzymes are proteins that catalyze chemical reactions without being used up or destroyed in the process Used in digestion, releasing of energy from nutrients for fuel, triggering reactions that build muscle and tissue

Regulation of metabolic processes

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HORMONES Hormones are chemical messengers that are made on one part of the body, but act on cells in other parts of the body Insulin - produced by the pancreas, which is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, muscle, and fat tissue to take up glucose from the blood, storing it as glycogen inside these tissues Glucagon produced by pancreas, raises the glucose level - causes the liver to convert stored glycogen into glucose, which is released into the bloodstream

Defense against infection

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The Immune Response is a series of steps your body takes to mount an attack against invaders Antibody (immunoglobin)-large Yshaped protein produced by B-cells that is used by the immune system to identify and neutralize foreign objects such as bacteria and viruses

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ACID-BASE BALANCE Proteins help to maintain a stable pH level in our body fluid by picking up extra hydrogen ions when conditions are acidic, and donating hydrogen ions when conditions are alkaline Otherwise, the resulting conditions of acidosis or alkalosis could lead to coma or death

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TRANSPORT Albumin transports a variety of nutrients such as calcium, zinc, and Vitamin B6 Hemoglobin transports O2 in the blood. Serum albumin transports fatty acids in the blood. Membrane transport proteins transport substances across cell membranes. Example: the glucose transporter

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ENERGY SOURCE If the diet does not provide enough energy, the body must begin to break down its own protein The proteins are broken down into individual amino acids, then deaminated, and the remaining carbon, hydrogen, and oxygen compounds are used to make energy or glucose If the diet contains too much protein, the excess will be converted to glucose, or stored as fat

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Transmission of hereditary characteristics

Nucleoprotein - conjugated protein consisting of a protein linked to a nucleic acid, either DNA or RNA

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Muscular Activity
proteins that allow cell and tissue movement Actin and myosin in muscle. Tubulin in the microtubules of the mitotic spindle or the eukaryotic cilium.

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Physical properties
Tasteless Colorless Amorphous Insoluble in fat solvents Varied degree of solubility in water, salt solution, dilute acids and alkalies Form non-diffusible colloids

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Solubility
Protein has definite solubility in a solution of
fixed salt concentration and pH Influence: 1) Effect of neutral salt increase solubility (salting in effect) in low concentration - high concentration cause precipitation (salting out) 2) Effect of pH minimum at isoelectric point and increase with increasing acidity and alkalinity 3) Effect of organic solvent diminish the solubility of proteins

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Chemical properties
Amphoteric Labile when subjected to alterations on pH, UV, heat, organic solvent Reactive and highly specific Precipitation Hydrolysis

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Denaturation
Any change that alters the unique threedimensional configuration of a protein molecule without causing a concomitant cleavage of the peptide bonds. Only the secondary and tertiary structure are affected, not the primary Proteins can undergo renaturation More viscous and no longer crystallizable

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precipitation
1) Acids or bases form insoluble salt due to amphoteric property - disrupt salt linkages
Tannic and picric acid - react with heterocyclic amino acids of proteins

2) Heavy metals Hg, Ag, Pb 3) Alcohol 4) Heating

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Hydrolysis
By dilute acids, alkalies, or enzymes and are broken down into fragments Addition of water

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Classification
1) Simple proteins are composed only of amino acids. -albumins, globulins, glutelins, prolamines 2) Conjugated proteins: proteins which form complexes with other substances Protein + carbohydrate: glycoprotein. Protein + nucleic acid: nucleoprotein. Protein + lipid: lipoprotein. Protein + a metal: metalloprotein. Protein with a phosphate group attached to one residues: phosphoprotein

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Derived protein - results from the decomposition of simple and conjugated proteins by the actions of heat and other physical forces or hydrolysis agents - rearrangement of within the molecules without breaking the peptide bond

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Test to detect the presence of proteins

Millons test - determination of tyrosine content in proteins - purple-red salt of mercury Biuret Test presence of peptide linkage - rose-pink to violet then purple Hopkins Cole reaction presence of an indole nucleus in the tryptophan component - violet ring at the junction Xanthoproteic reaction benzene ring - yellow with acid and turns to orange when treated with base

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Test for SH group protein with cystine, cysteine or methionine - black precipitate Molischs test presence of glycoprotein - violet ring Ninhydrin reaction - typical for -amino acids - react with ninhydrin reagent yielding CO2, aldehyde and a blue colored complex compound:

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Amino acids general structure

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Classification by R group
Based on the polarity of R and interaction with water 1) Non-polar, aliphatic R group

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2) Aromatic R group nonplar, hydrophobic interaction , absorbs UV

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3) polar, uncharged R group soluble in water

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4) Positively charged (basic) R group

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5) Negatively charged (acidic) R group

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Physical properties of amino acid

White crystalline substance Soluble in cold water Insoluble in alcohol and ether Most are sweet, some are bitter and tasteless

Chemical properties
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Optically active due to the chiral carbon - can exist in iether D- o Lenantiomerric form Amphoteric salt like character also called inner salt of zwitterion occur in isoelectric point - intramolecular neutralization reaction

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Characteristic titration curves

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Form esters with alcohol Amino acids can be acytylated, benzylated, methylated in the presence of acetic acid React with nitrous acid, liberation of nitrogen gas Formaldehyde reaction with an excess of neutral formaldehyde is added to neutral amino acid solution, a distinctly acid mixture is produced Heating with barium hydroxide- primary amines are formed due to the breaking of carboxyl group with the formation of CO2

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Nutritional properties
Essential amino acids are those that cannot be synthesized in the body at a rate sufficient to meet the growth and maintenance requirements. They must provided preformed in the diet. Nonessential amino acids- are those that can be synthesized in the body from an available source of nitrogen and a carbon skeleton. They mixed diets contain ample amount of both essential and nonessential amino acids.

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Base on their amino acids content , foods are often classified as sources of: Complete protein - contains all the essential amino acids in proportions capable of maintaining life and supporting a normal rate of growth. (high biologic value proteins) ex. Egg, milk, meat , fish and poultry. Partially complete protein- contains all the essential amino acids but a relatively small amount of some of the amino acids necessary for growth. Ex. Gliadin and hordein. Totally incomplete protein lacks 1 or more of the essential amino acids therefore incapable of replacing or building new tissues, hence cannot support life or growth. Ex. Are zein or gelatin.

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Factors Affecting Protein Requirements Body weight based on BDW Growth infant and adolescent need more Pregnancy Lactation Aging higher as become old Nutritional status Protein quality

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Sources of Protein Animal Sources: - eggs, milk, and milk products, meat , fish, poultry, and sea foods. Plant Sources: - cereals( wheat, rice ,corn); legumes(mongo beans, peas, soy beans, white beans, red beans, lentils, lima beans, nuts, processed vegetables proteins

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Protein malnutrition
Liberal protein intake consumption of a high protein diet is wasteful since the body does not store protein in the sense that it stores other nutrients. Protein deficiency Kwasiorkor - ( meaning the displaced child) occurs in children shortly after weaning when the diet is high in starch and low in quality and quantity of protein Marasmus ( wasting or withering). Is usually seen at a somewhat earlier age than kwashiorkor