I giuf,erd n-cyel-giYX is cleihctnayl sinedcdroe a a“rpyrim omain cdia tustcurer of a et”onpri nices eht inetidfoni fo a iarPyrm eusrrttcu fo a nipotre is “a alerin hcina of anmio cd.as”i If ouy msse htwi hte ryarmPi stureturc, as ni the sutioeqn mse,t you nctaon form the dSeacrnoy tscretruu fo teh ne,tpoir hiwhc is mdtidneree yb teh yeonhgddbrnniog- hwhic cosrcu ebeetnw eth ipetped knebaocb, enieednndpt of eht R .pgruso I poeh htsi daem e.esns
rFom daiwikpie: dernaoyc“S tesururct is frmallyo dienedf by eht rnaptte fo rhgondye onsbd weetebn het maoni gynhdroe adn xlroaybc goxyen satmo ni eth pdpeite ecbokbna.” ihpesams( eimn)
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 gsuy dna i equot mfro aculs/ee.opswwfgdo-pehtrs:/0peebitailserth1is4trt2/seom/n/.oicmtwoct
09"% vahe na lntdiiebfiae cgetein tnatioum LC
O A11 nda OCL 12A
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nalbramo ngelaocl iikosgnns-lrc avi a lyngeci utsbtusintoi in eth cllponoraeg uceomlel "
cihhw snmea that IO hsa a ylgneci oinsstubtitu nda ehetorfr sti unable ot ofrm a nreosaydc ururcesutt.
Deu to lsn'iceyg allsm z,sie ti sceraet k""knis ni het oiman cdia qee.ensuc eehsT kskni aer eedden to ctcolyrre romf eth csdyareno rrtcs.ueut
hteOr ser:nasw
-XylYG- is oacebnbk fro gcnoalel plaha .ichna 3 nagcoell ahlap chiasn iapsrl ot rfmo eprtli x.lhei yeicGnl sah no R pugor, nolagwli ofr tfilixilyeb adn afootrimn of erlipt h.xlie oN eicglny pvresnet siht isnuctuoon saiginlr,p nengpteivr eht tnorfomia of aelcongl sorecdnya tru.certsu
aRllce ttah lhe-acahleisp dan setetes-hab ear xmspeeal fo coaydrnse tutsesrcu.r isTh nac eb othuhgt of a mainastntofei of hte palha .hixel
eoNrthA ayw to etg at it is vai :timioaielnn
A. eordyghn nngdibo tduolwn really heacgn ciens eehtirn nelnaia rno eilgnyc rea Barol .p yGl g;t& Aal sd'htulon gahnec ohw noieplr si eoifdidm (I anem ti OCUD,L if herte swa a tciesr cnrdehina ro tm,ieohngs utb nto a retag rDna s)w.e ghntino to icteiand hatt lcoangle gientdeorda is eetrald ni espsroen ot na AA iuostb.tintsu ols,A in het ntecxto of OI whi(ch si teh enerstipgn )naotplmic, we eardyla nkow that eth mrleobp ndeos't avhe tinghnay to do hwit da,deorgietn eomr hwti het ahncge in uf.icutrno tuecsrt/En oHlnstye ntd'o .wkno
s’reHe eno yaw ot sclnirsetofia-emoe-p ddrece“eas rnbo-hndydgoe tfrmo:n”iao Im’ not a gbi nfa of tish leni of nn,asgerio ubt ntaccylihle aealinn as a idse pogur hsa oerm ohensg*dry rof tpaleinot nyhrgeod onbidgn hatn gilyecn:
nnla:eia —C3H
:ylgenci H—
S,o ah”licyceltn,“ ainnlea wdoul irtepm erom bddeogo-nhnry ,iomnaorft wihhc gimth alwol uoy to lnimiaete thta icohe.c
tTha idas, it esems tlasom mboiplessi ot eulr tuo hoittw(u yrev lchctenia lgdnoeekw ro msoe vpdodeir laptneriexem atad) atth eht slilgyht grreal nlnaeai edso not mpiiar ongyhedr dboinng enbwtee llancego umelscole avi stcrie )ais(tapl reectre.innef In irmplse trms,e eicsn lneiana is er,aglr ouy odwlu kniht htta ti stum owhsmoe eefreirnt with eth e-onihnodrygdnbg tath soccru hiwt teh detypwil- eylginc.
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lt*tryiSc nkgeasip, s’it not eth umbren fo ngerhdyos utb aols eht rtnehtsg of het eliopd thta tfitclsiaea ndeoyrgh dg:noibn a yodhenrg obudn ot a tosnrlyg eeglentvicaetro loelmuce leki ifnluore will rap”“aep rmoe peoisvit and, ,thus dyor-odehnnbg emro tlgsrony thiw a beynar gonexy maecpdro( wthi a oendgyrh eenotdccn ot rncao,b rfo e.empal)x
trFheru dn:igear
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 tighm be tihiveornngk ti ut,b H nbdo monatofri of a'sa kemas eth noarcesdy rtuercust of eht opetinr lalcngo(e in hsit es)a.c heT Gyl ot Aal iosnibttuust edso srtlue in sles H nobd no,itfmrao tub fo dudinailvi aa's not ebeentw oganlelc lcleosuem t(hta imthg be rome fro naaryequtr sturr)tceu
yPirarm ucuertrts = monia aicd d euSseccnenaqreoy trutcusre = rsectrutu roemdf wthi a neglis aoinm aicd ncueeseq a(ebt paedtel th,ese hpaal xil,eh ryi )rtetceTa rtrseuutc = lpulimte adceonysr utrcstseur tiingnceart trheoetg tlu(pieml baet eelatdp ehsset adtecks no pot of ahce eht,ro teQy)rcanaruetr rtetusurc = rientop utctsreru ferdom frmo dolfing of lal iayrertt usscruttre to kame gnibdin tesis, .etc
Scnie eth naliean saw tup in caple fo het ,neyGilc the yrmirap cruuttser aws nluabe to fmor na phaal ehixl iensc palah hxeli srcetruust eedn a trraaciupl equensce yg(l - -x )y in eordr to mrof edhnogyr sobnd ot kpee eth xheil ts.blea
what si eancogll ? a enyasodrc oeniptr rurtu.tsce
hewn ouy movree nci,ygle hte stmo anbdnaut naomi aidc , rfmo eth csrueprro lceulmoe liwl oyu egt a reprop nosyearcd usterctur ? NO
Gyl is l,aopr Aaneiln si orlnpona nda odyo.hiphbcr Messsien nrivenovtaocsen u.oimntat seeTh AsA have rdnietffe ielcamhc srtrppieeo hwich ldae to editrudsp ntpiero ldgifon oaeyrcd(ns sucerr)t.tu mlriiaS to uGl - alV bittuituosns ni iceSkl lleC i.seeasD
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$279$49I khnit ti sah isnemtohg ot od ithw ilnygec (deu to tis lsmal zise it cna ift in amny lcpase ehrwe htroe nioma aidsc nac nto dna cehne it doevprsi srtlcuuar“t ”oeccspstnma ot the lolcena,g ei.. tup a kikn ni het pahla ).heixl If eglyicn is ieplcmasd by getsimhon ,eesl I d’ton hinkt golcop-naler nac mfro sti ortcerc yrscaodne uer.cttsur
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