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AMINO ACIDS & PROTEINS

PROTEIN STRUCTURE
STRUCTURE OF PROTEINS ARE ORGANIZED AT 4 DIFFERENT LEVELS: PRIMARY SECONDARY TERTIARY QUATENARY

PRIMARY STRUCTURE

THE NUMBER OF AMINO ACIDS IN A STRAIGHT POLYPEPTIDE CHAIN IS CALLED PRIMARY STRUCTURE OF PROTEINS.

SECONDARY THE FOLDING OF POLYPEPTIDE CHAINS INTO SPECIFIC COILED STRUCTURE HELD TOGETHER BY DISULFIDE AND HYDROGEN BONDS IS CALLED SECONDARY STRUCTURE OF PROTEINS. EXAMPLES: ALPHA HELIX BETA PLEATED SHEETS

ALPHA HELIX COLLAGEN

BETA PLEATED SHEETS KERATIN

TERTIARY THE ARRANGEMENT & INTER RELATIONSHIP OF THE COILED STRUCTURE INTO SPECIFIC LAYERS OF FIBERS IS CALLED TERTIARY STRUCTURE OF PROTEINS

QUATENARY SEVERAL MONOMERIC UNITS EACH WITH APPROPRIATE PRIMARY, SECONDARY & QUATENARY STRUCTURE MAY COMBINE TOGETHER & FORM QUATENARY STRUCTURE OF PROTEINS

SOURCES OF PROTEINS
ANIMAL SOURCES:
FISH EGG MILK

PLANT SOURCES
PULSES LEGUMES WHEAT

FIRST CLASS PROTEINS


PROTEINS THAT CONTAIN ALL THE ESSENTIAL AMINO ACIDS EXAMPLE PROTEINS FROM ANIMAL SOURCES

SECOND CLASS PROTEINS


PROTEINS THAT DO NOT CONTAIN ALL THE ESSENTIAL AMINO ACIDS EXAMPLE PROTEINS FROM PLANT SOURCES

CLASSIFICATION OF PROTEINS
PHYSIOCHEMICAL
SIMPLE COMPOUND DERIVED

FUNCTIONAL
CATALYTIC TRANSPORT STORGAE

STRUCTURAL
GLOBULAR FIBROUS

SIMPLE PROTEINS
Upon hydrolysis they yield only amino acids
ALBUMIN GLOBULIN GLOBIN PROLAMIN PROTAMIN HISTONES ALBUMINOIDS

ALBUMIN
Synthesized only in the liver. Water soluble Coagulated by heat Has carrier functions in the blood e.g.; Ca++, bile salts, bilirubin, fatty acids, steroids etc. Exerts oncotic pressure in the plasma. Deficiency results in the loss of carrier functions, and decreased oncotic pressure results in edema etc.

GLOBULIN
Synthesized in the liver and the spleen Water insoluble Alpha and Beta fraction has carrier functions like transferin. Y- fraction has defensive functions like yglobulins Exerts oncotic pressure in the plasma. Deficiency results in the y-globulins results in decrease production of antibodies making the patient vulnerable infections

GLOBIN
It is the protein part of the hemoglobin. Normal adult hemoglobin is composed of four globin chains that is two identical alpha and two identical beta chains. Deficiency of any of the globin chains results in thalesemia. Mutation of the beta chain at carbon no.6 where Glutamic acid is replaced by valine results in Sickle Cell Anemia.

ASSIGNMENT ASSESSMENT
DEFINITIONS NEED TO BE EXACT GRAMMATICAL ERRORS SENTENCE FORMATION NEATNESS CLARITY PRESENTATION SEQUENCE OF ANSWERING INCOMPLETE ANSWERS/MISSING PARTS COPY & PASTE TECHNIQUE DIAGRAM SPACE AND DESIGN STAYING WITHIN THE TOPIC ASKED SPACING ANSWERS MISSING PHOTOS

OBJECTIVE OF ASSIGNMENT
TO ENHANCE YOUR GRIP OF THE SUBJECT TO GIVE AN IDEA OF:
WHAT IS IMPORTANT HOW QUESTIONS ARE DESIGNED HOW TO FORMULATE ANSWERS

THIS NEEDS INPUT OF TIME AND ENERGY NOT JUST SUBMITTING IT AS A FORMALITY!!

PROLAMIN They are storage proteins for nutritional a purpose that is gliadin of wheat, zein of maize etc. HISTONES Combines with nucleic acids to form nucleoproteins They are basic proteins because they are rich in arginine

PROTAMIN Combines with nucleic acids to form nucleoproteins They are present in sperm cells. ALBUMINOIDS They are known as scleroprotein. They are fibrous proteins with great stability and form supporting structures OF 3 TYPES:
KERATIN COLLAGEN ELASTIN

KERATIN
Present in hair, nails, hoofs and feathers. Outer most layer of the skin is keratin and it is soft and is known as Pseudokeratin

COLLAGEN
It can be stretched Found in the connective tissue and bones as long, thin, partially crystalline substances. Though it is an animal protein but nutritionally it is poor because it lacks tryptophan Acts as a rigid rod consisting of three polypeptide chains wound around each other by cross links to form a three stranded rope lie structure. In old age the cross links become more na d more resulting in stiffening of the muscles and joints.

Collagen can be converted into gelatin on boiling with acid water. Gelatin is easily digestible by the protein but poor nutritionally. Mutation in the synthesis and processing of the collagen occurs in Ethers-Danlos Syndrome, which is characterized by the abnormalities blood vessels, skins, ligaments and internal organs

ELASTIN
Present in the yellow elastic fiber of connective tissues, ligaments, tendons and blood plasma. Formed in large amount in the uterus. Hydrolyzed by pancreatic enzyme elastase

COMPOUND PROTEINS
Upon hydrolysis besides amino acids, they also yield non-proteinous substances that is the prosthetic group. They include:
NUCLEOPROTEINS PHOSPHOPROTEINS LIPOPROTEINS CARBOHYDRATE CONTAINING PROTEINS CHROMPROTEINS METALLO PROTEINS

DERIVEDPROTEINS
DERIVED FROM SIMPLE OR COMPOUND PROTEINS BY DENATURATION OR HYDROLYSIS THEY INCLUDE:
PRIMARY DERIVED PROTEINS SECONDARY DERIVED PROTEINS

Primary Derived Proteins


These are denatured proteins. Denaturation is a process of unfolding and disorganization of proteins. Denaturation can be done by heat, x-rays, extremes of ph, salts of heavy metals, urea. Denatured dietary proteins are easily digestible.

Secondary Derived Proteins


They are obtained by hydrolysis of compound proteins that is proteoses, peptones and oligopeptides( that is dipeptides, tripeptides and tetra peptides)

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