Proteins “The precise folding up of @ protein into its tertiary structure (creates a three dimensional arangement of te acive groups. “The way each group faces wit respect othe others gives te protein its unique chemical properties. a protein loses this Precise structure (denaturation), itis usually unable to carry is botogcal function. Proteins are often classifiod on tha bas Structure (globular vs fbrous). Some of the properties used the basis of structural classification aro culned oppost, Primary Structure - 1° (aminoacid sequence) Shigeo undies amino ate i gener nh patie _ bonds to form molecules calles polypeptide chains, There are 20 Swe ines tf ante ads han be lla npser na vat tuber oar orator. Th seaueee cles re Drimery atuctre I's te arargement ot eacton ard eeosongarts min arin so cma eres a ghae ‘fret opansston a pret enatcege Kon ‘Secondary Structure - 2° (a-helx or B-pleated sheet) Dolypontdee socom flies varus wae, retamed 6 ae the ‘Secondary 2) sete Th most sornman yee of actres ‘a acaled whelk and a pleated sheet. Seconcaryeracures fare maintained with hydrogen bands between neighboring CO. land NH groups. H-2oncs,athoughinsiualy weak, provise Consiecabe stergth when thee ae a larga camber of her, ‘Tha example, igi. shows the two main types oF secondary structure. n bo the side groups [rot shown) project out trom the aructur. Most lobule posin contain regions of«- aloes togethor with shoots. Koratn (a fbrous prot) Ie composed aimaat ently ofa heloos, Fboin (tk preter), ‘nator ferousrcton, almost ntl insect form. Tertiary Structure - 3° (toiding) Every pron has a.precse src formed by he cing of the sncondary structure ino & complex shape cated the tertiary ‘trueture. The prot folds up because varius pons onthe secondary sruture aie tracted 1 one anoter. The strongest {ks ne cautes ty bonding between nachnotrg cystine amo acti whie orm deautie Seen Other erections tat are woven folding incuge ek onc and yrogen bonds as we ashyerophebe reeacters. ‘Quaternary Structure - 4° Some proteins (uch as enzymes) are complete ara funciona wih a tora sireture only. However, mary complex protens x38 egotepsins of poypepce chains. Tre arengement of ‘he petypepide chains nto a functional proteins termed the _quaterary structure. Tre example (gh) stows a molecule ot emogbbn, a enulr prken ooToosed of 4 polpenie stuns “pos togetrer: wo genes! Bets ehams an 9 isa alpha ‘Shain Each has ahame (ion senaring) grup athe core ‘ho chain, ahien ings cxygen.Prcane canting ron peta ‘ator are eonjugeed protsina, Tho non poten pase the rostneie group, Denaturation of Proteins Derturation refers 0 he loss of he twee-dmensoal sre {ang usuly aco ebesogial uncon) ofa proton. Derauation 's often, athough not avaye, permanent. t resus trom an _aterabon ofthe bonds thal mania Ye secondary and teraty Suds clthe poten even thaughte sequence of amino ais “femansuncnanged, Agen that cause denuraton ae: *'Sirong acide and alkalis: Disrupt ionic bonde ard esl 0 naguletor of he rata Lang execaure also Breaks down {he pmary suc cho pre. + Heavy metas May arp enc tends, fm stor bonds wih ‘pe caeonyl gun ol he cup, and redo prota charge. ‘The general ele isto cause tne procpiaton ofthe pci. + Heat and redaton(e3. UV): Cause disuption ofthe bonds ‘he pct vag incensed anergy proviso sams. + Detocgents and solvents: For bonds withthe non-polar oun i he prota, thereby dung hydrogen boring. + ‘Amino seid sequence 2 y Foarogen ons ‘Trees! sbape 8 ystogen bonds septa ‘Alpha (a) helix or frpleated sheet 3 louie bre Polypeptide chain a - Beato: spa cen Hemoglobin molecule —intemaitin exh otypepieencises en te Sonar oresrate gue Hemoglobin's Chemical Formula CC scsy H sais O are N ray S Fe,‘cotiagen consists of twee nea! pelypeptidee wound around each ‘ther 6 form ate" Evry tie ‘amine eld mean peypartt falyeine (Gly) malecule. whe I} eeogen borg ccc hek ‘ree sand logtner Bovine insu is relatively smal rosin consisting ot ‘wo polypepide chars anv chin ania cha). These ‘wc chains are hed ogenr by csi ridge Sabie rsgnooring cystine (Cys) molecules * Sretly explain how proteins are involved inthe following functional roles: {@) Structural issues of the body: (©) Reguiating body processes: (6) Contractile elements: {@) Immunological response to pathogens: {(¢) Tansporting molecules within colls and in the bloodstream: (9) Catalyzing metabolic reactions in cals: Explain haw denaturation destrays protein function: & |S. Describe one structural ference between globular and fibrous proteins: “4 Determine the total number of amino acids inthe « and 6 chains ofthe insulin molecule illustrated above: Patan RaAmino Acids ‘Amino acids are the basic units from which proteins are amino acids) trom their det. Al ther amino acide ca made, Plants can manufacture all the amino acids they constructed from these essential amino acids. The oro=" require from simpler molecules, but animals must obtain @ which the diferent amino acids are linked together to © certain number of ready-made amino acids (called essential proteins is controlled by genes on the chromosomes. Properties of Amino Acids TRE pep cn rm Tivee examples of amine aces wih gee amos citerent chevicelproperies ave shown Gat fameesocteate alia Propory i rm win helt specie Fr groups farina Te F groups can have qu Aveo eremcal roperte Cysteine Lysine ‘Aspartic acid “The ater of amino actsina pot |s ected by he oer of rucooiesn ONA and mRNA. Peptide bonds lnk amino eds {get in ong pore eaes povpootde hans 200 moy fom | parterall ofa prota, ‘The amine aide aro inked together by peptide bonde to form eng chain of upto several hunared amino acids (caled sokypopts chins). ‘These chains may bo functional unis (complete by themsehves) or they ‘may need tobe jones to other polpeptise chains before they can cay ‘out heeft, Inhumans, nt al amino acids can be manuiactured by our body en must be ten in wih our cat eight n adults). These {ara the essontial amino acid’ (ndcated bythe symbol @ onthe ah “T Dasorbe the biological functions of amino acids: 2. Desorite what makes each of the 20 amino acids unique: ‘3. Name the type of bond that links amino acids together:Condensation and Hydrolysis Reactions 2 acid can combine to form opto chain in what is a 2. eondeneationrsacion Pete ane canbe broken Hy ee o by hydrolysis ts smols amie acs SN-G-c: IN-C-c% 2 amino pa Lee ane Amino seid Amino acia A Hydrolysis reaction When 8 alpepie ie pit 5 became procoes of Algcaten, 2 water molocula provides a rydrogen ane a cron croup ig Ho Dipeptige “ater Pepto ter Dipeptice ‘Describe the process that determines the sequence in which amino acids are liked together to form polypeptide chains: Explain what is moant by essential amino acids: ‘Deserve briefly the process of the condensation reaction for amino acids: DDesoribe briefly the proness ofthe hydralysis reaction for amino acs: 8 Name the optical isomeric form that occurs in nearly all amino acids in ving things: