Biology Unit 1

Topic 2: Genes and Health

PROTEIN ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ Students will be assessed on their ability to: 1) Describe the basic structure of amino acid 2) Describe the formation of polypeptides and proteins 3) Explain the significance of a proteins primary structure in determining its threedimensional structure and properties ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ I II Introd ction Organic compounds consists of C, H, O and N and sometimes S and P Not truly soluble form colloid !tr ct re o" #$ino #cids There are twenty amino acids commonly found in proteins !ery amino acid has at least one amino group "#NH $% and one carbo&yl group "#COOH% The carbon atom ne&t to the carbo&yl group is the #carbon atom ' hydrogen atom and an ( group are bonded to the #carbon atom The !arious amino acid differ in the nature of the ( group # Neutral one amino and carbo&yl group # )asic more amino than carbo&yl group "e*g* lysine% # 'cidic more carbo&yl than amino group "e*g* aspartic acid% # +ncharged polar contain sulphydryl group "#SH% e*g* cystein or hydro&yl group "# OH% e*g serine # Non#polar contain hydrophobic hydrocarbons e*g* leucine

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Properties o" #$ino #cids Soluble in water but not in organic sol!ent ,orm %&itterions in neutral a-ueous medium where the amino group pic. up H / and become NH0/, the carbo&yl group lose H/ and become COO# thus the amino acid has both positi!e and negati!e charges )eing a$photeric amino acids can act either as acids or bases therefore they can act as buffer which resist changes in pH when small amount of acid or al.ali is added

Biology Unit 1

Topic 2: Genes and Health

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(or$ation o" Polypeptide 'mino acids are 1oined together to form proteins Combination of two amino acids in!ol!ed condensation reaction between the carbo&yl group of one amino acid and the amino group of another and a water molecule is remo!ed The two amino acids become 1oined by a peptide bond to form a dipeptide 2t possesses a free amino group at one end and a free carbo&yl group at the other

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Types o" Bonding in Polypeptides ach polypeptide has a specific three dimensional shape which is important for its function This shape is due to four types of bonds which occur between !arious ( groups of amino acid residues in the polypeptide chain Hydrogen Bond ,ormed between hydrogen atoms "small positi!e charge% and o&ygen or nitrogen atoms "small negati!e charge% within the polypeptide chains ach hydrogen bond is !ery wea. but the great number of bonds contribute to considerable stability of a polypeptide molecule Ionic Bond 'dditional NH0/ groups in basic amino acids and COO# groups in acidic amino acids may form ionic bonds 2onic bonds can be bro.en by changing the pH of the medium around the polypeptide *is lphide Bond 'rises between SH groups on any two cysteine residues The sulphydryl groups of two cystein residues are o&idised and subse-uently form a disulphide bond Hydropho,ic Interaction 2nteractions between hydrophobic ( groups The protein folds so as to shield hydrophobic ( groups from the a-ueous surroundings

Biology Unit 1

Topic 2: Genes and Health

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!tr ct re o" Proteins Pri$ary !tr ct re The number and se-uence of amino acids in a polypeptide +ni-ue to each and e!ery polypeptide chain The se-uence of amino acids determines all the properties and shape of the protein Only peptide bond is responsible at this le!el of protein structure !econdary !tr ct re The #heli& and #pleated sheet Stabilised by hydrogen bonds formed at peptide bonds ( groups of amino acids are not in!ol!ed in maintaining secondary structure Tertiary !tr ct re The bending and twisting of the secondary structure into three dimensional configuration ,our types of intramolecular bonds "hydrogen bond, ionic bond, disulphide bond and hydrophobic interaction% maintain the tertiary structure - aternary !tr ct re Combination of a number of polypeptide chains and associated non#protein groups into a large, comple& and functional protein molecule ach polypeptide chain is called a subunit and the subunits are held together by hydrogen bonds, ionic bonds and hydrophobic interactions

Biology Unit 1

Topic 2: Genes and Health

3e!els of protein structure

Biology Unit 1

Topic 2: Genes and Health

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.lassi"ication o" Proteins #ccording to !tr ct re (i,ro s Protein 3ong polypeptide chains form long fibres or sheet running parallel to one another and lin.ed by cross bridges Secondary structure most important "little 4 no tertiary structure% Primary structure of regular repetiti!e se-uences 5ater insoluble due to large number of hydrophobic ( groups on the e&terior of the molecule *g* Collagen # a component of connecti!e tissue e*g* s.in, bones, blood !essels and teeth* # consists of three polypeptide chains each about 6777 amino acid residues long # three chains wind around each other to form triple heli/ structure # rich in glycine and proline residues # collagen is a good str ct ral protein because8 # it is insol ,le in water due to large molecular si9e and the hydrophobic nature of the amino acid residues # it has great tensile strength as the polypeptide chains are organised into big bundles three polypeptide chains are cross#lin.ed to each other to form triple heli& with hydrogen bonds between ad1acent chains, triple helices again cross#lin.ed to form collagen fibres Glo, lar Protein 3ong polypeptide chain tightly folded to form spherical shape Tertiary structure most important Primary structure of highly irregular amino acid se-uence 5ater soluble due to the hydrophilic ( groups 1utting outward from the molecule *g* 2nsulin # a small protein in!ol!ed with the control of blood glucose le!el produced in cells of islets of 3angerhans in the pancreas # consisting of two polypeptide chains held by disulphide bridges # insulin is a hormone8 # it is sol ,le in water so it can be transported in the blood due to its small si9e and hydrophilic nature of the amino acid residues

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globular structure

fibrous "or filamentous% structure