I udgei,rf ygXl-Ye-cni is thcllenciya cerdiseodn a iay“mprr inoma iacd cuserrutt of a rin”toep niesc eht intnoifedi of a arirPmy cetrtrusu of a pritneo is a“ alrein nciah of iaonm c”.asdi If yuo sesm thwi eht iPrryam etsc,uturr as in teh ouitqnse tse,m uoy nntcoa form hte acyrSeond sueuctrrt of het topi,ern ihwch si ienmdderet yb teh igor-denygnnbdho cwhih srcouc ebentwe the peeiptd nebacbko, depednintne of eht R rso.gup I hepo isht amed ssene.
mFor edwiaikpi: dro“Seycan uructstre si yroalmlf fineded yb teh etparnt fo nedorhgy nobsd weenbet eht onmai ydgoehrn dna xoabylrc gxeyno moats ni the iptdpee bbknecoa”. espmashi( m)ine
From Molecular Biology of the Cell:
Biologists distinguish four levels of organization in the structure of a protein. The amino acid sequence is known as the primary structure of the protein. Stretches of polypeptide chain that form α helices and β sheets constitute the protein’s secondary structure. The full three-dimensional organization of a polypeptide chain is sometimes referred to as the protein’s tertiary structure, and if a particular protein molecule is formed as a complex of more than one polypeptide chain, the complete structure is designated as the quaternary structure.
ok ugys nda i teqou ofrm ds/mectoe/reti0sshowit/e2poopi-cp.tgtamb/c:if/ah.relrsntwelout1essw4
"%09 veha na anetiilbefid genciet taunoimt L
OC A11 and CLO 1A2
uessa
c balonrma gonalcel nlsgciikrnos- avi a ecgnlyi sittstniouub ni eht gocleaplrno lmcoulee "
wichh neams thta IO has a ienglyc uutiitbstnso dan eorfther tis aulebn ot orfm a ocaynesdr ruttcuur.es
ueD to ges'ilnyc mlsal ,sezi ti tscerea ni"skk" in the iaonm icda neqecesu. seTeh nsikk aer ddeeen to erclortcy frmo het erocnadsy rertuucs.t
Oehtr :rsnwsae
GX-lYy- si eoncbabk rfo olncglae apalh c.nhai 3 ngoceall haapl cinsah slarpi ot morf ierptl l.xeih lciGnye ahs no R upog,r willgaon orf eitlyiblixf nad trnoamoif fo ritpel helix. No enicgly vnpeerts ihts cinountsuo aglsii,pnr vpentignre teh nmoitfaro fo algenolc yadscoren trreucsut.
aRlecl tath -elilacshphae nad b-sseehetat ear elpsemax of erosnacyd .urestrsutc hsiT can be ghohttu fo a sainmationfet of het palha i.exhl
NrhAeto yaw ot get at it is iva toinmln:ieia
A. roydenhg donbgni wltnduo llraye naeghc neisc niehtre naeinal nro glicyen rea .opaBrl Gyl tg&; lAa hn'tusodl ghcean woh oinpelr is idomfdei (I anem it ,LDOCU fi rhete was a icters hnedrinca ro sthim,goen but nto a eatrg arewn. )sD nhnogit ot naictedi thta caoellng eddagitneor si tlareed in eposnsre ot an AA tu.tisstuniob sA,lo in teh ntxoetc fo IO iw(hch is hte gepetnsinr lmt,can)oip ew dlraaey wonk hatt eht meprbol 'dosten evah ngyhtain to od hwti ,ertdodgeina remo tiwh teh hceang in Esrtcut .furioctu/nne tlnoeHys nt'do w.okn
H’seer neo way ot opoiceisr-smenleatf- “dcdreesea dh-orneynogbd roofm:itna” I’m tno a gib anf fo ihst ienl fo ergnnoia,s tub cyiltalhecn naenlai as a side rgopu sha mero eyhod*nsrg rfo elitnaopt royndegh gbdnion ahtn ycienlg:
a:ennali —CH3
g:nylcie H—
oS, c,t”ihalelc“ny eainaln odwlu ritpem rmoe -boddynegonhr ot,oimrnaf whihc gimht lwlao you ot ineltmiea taht cioc.he
Ttah asid, ti sesme mtalso olpmsisibe ot urle uot (wotuiht vyer lcnehicta onedlgewk ro esom vdedproi xmeetpeirlan taad) htta het hglitsyl raergl iaanenl sdoe nto mpiair nrhoygde dninogb weenebt loleganc mesloucle aiv rstiec l(at)saip re.nrifeeetnc In elprsim ,emstr sneic laennia is are,grl oyu lwduo hnkit htat it tsmu hwemoos nretiefre hwit teh nendoorbghnygdi- htat csoucr with eht ditl-ywep cigleny.
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t*tSrclyi nsa,pegik si’t ton teh rmnbeu of oeydrghsn btu osla the ghtestrn of eth ieodpl ttah taecflatsii hnreydgo dgninb:o a nhdgyreo bdonu to a tnrygsol ilotreevcaenteg cluoelem klie fueorlni iwll ”eparpa“ more ipsteoiv and, stuh, ryddbeooghnn- moer tnryslog twhi a rebnay xygoen ed(macpro whit a ygnehdro eetconcdn to ,bnrcao rof empx.)ela
errFthu aiedg:rn
From Molecular Biology of the Cell:
Hydroxylysines and hydroxyprolines are infrequently found in other animal proteins, although hydroxyproline is abundant in some proteins in the plant cell wall. In collagen, the hydroxyl groups of these amino acids are thought to form interchain hydrogen bonds that help stabilize the triple-stranded helix. Conditions that prevent proline hydroxylation, such as a deficiency of ascorbic acid (vitamin C), have serious consequences. (Emphasis mine)
From Molecular Biology of the Cell:
The primary feature of a typical collagen molecule is its long, stiff, triple-stranded helical structure, in which three collagen polypeptide chains, called α chains, are wound around one another in a ropelike superhelix (Figure 19-43). Collagens are extremely rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Proline, because of its ring structure, stabilizes the helical conformation in each α chain, while glycine is regularly spaced at every third residue throughout the central region of the α chain. Being the smallest amino acid (having only a hydrogen atom as a side chain), glycine allows the three helical α chains to pack tightly together to form the final collagen superhelix (see Figure 19-43).
I ithgm be nonitekivhrg it b,ut H ndbo otamironf fo as'a sakem teh rsyodaenc tstrucure of het preoitn ol(lecnag ni isth )a.sce ehT lyG to Aal snutotstibui osde rstleu ni sels H ondb rmnfoa,tio but of anuddlviii 'asa otn tbeewen laonglec uoemelscl a(htt timgh be eomr rfo auaerqtynr erctsru)tu
raPmriy tururstec = amoni dica o csqeeredSucnyena utcrtesur = tsrtucreu reofmd ihtw a eignsl aoinm daci neequces abe(t adpeelt tee,hs lpaha ix,ehl ectT yrta)rie rurtstceu = tllmpeui ecaynrsod ctsserutru ntneiictgar hgottere uile(tlmp ebat peleadt sesthe dasektc no pot fo aech tre,ho uet)arty Qcnrrea crttrsuue = tprenio curtruets rmfoed ofmr findolg of lla rrateity rscustetur to meak bndiing ,tiess c.te
cSnei teh laianne wsa tpu in pecla of teh ylnic,eG teh marpiry teururcts aws bnluae ot fmor an lapha eilhx cinse haalp helix eurttcsrsu dene a cuprrilaat eeesuqcn g(ly - -x )y ni oredr ot mrfo ondhregy osbdn ot ekep hte hxeil seb.tla
tahw si nleoaglc ? a cdeaoyrns tipeorn .eucrttrsu
when ouy ovmeer gni,ecly teh otms danaubnt anomi icda , mfro eht cperrrsou eeumcoll iwll yuo gte a prpreo arcsdenyo estucutrr ? ON
lyG si a,lorp aeinlAn is loapornn dan i.bphdocroyh snseiesM vcevniaesrnnoot a.tonimtu Tshee AsA avhe fireedtnf meiccalh seirrpetop chhiw dlea ot deirsdtup pinoert gnidflo cseonar(yd tu)utrsre.c limraSi to uGl - Vla uttbiustsoin ni ckiSel ellC se.iesaD
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$279$49I think it ahs tnmsehiog ot do htiw lyicneg (ude to sti lamsl ezsi it nac fit ni ymna psacle ehwre rteho ioamn scida acn otn dan hecne ti esdvipor ut“rralctus opscs”eactnm ot teh ogn,cleal i.e. ptu a nkik in teh aaplh xh.li)e fI negylci is pciasmdel by nstihmgoe l,see I on’td htnki eoaolgrp-nlc cna rmof tsi tecrorc nsoadycre crruts.teu
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