I fdgie,ur X--lncgieYy si caceniltlyh ddisnercoe a rpmria“y minao daci suttcruer of a opretn”i nceis het tdnoienifi of a miyPrra erututscr of a ntroipe si a“ aienrl ahnic of maoin .cd”asi fI uoy esms ithw het yPimarr ruurct,tes sa ni hte teniouqs et,ms uoy nocatn fmor het roecSadyn rsettruuc fo teh p,entoir ciwhh is eednditrem yb eth hegndngdo-rbynio ichwh ocsucr tenebwe hte pdieetp ncboebak, eineetnddnp fo teh R .spugro I peho ihts aemd ese.ns
Fomr keaiidwpi: “ryeoaScdn rsuerctut si lflarmyo dniefde yb hte neptrat of dhoyrgen sndob eewebtn het oanim orygndhe dan yloarbcx nxyego satmo ni het pepedti cbabeokn”. pesh(iams nmie)
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 ygus nda i oqeut mfor udtewei:w0fssot4cehres/etom/tl.piontmbtawcrs2-iogitpps.clrsha/ee//o1
"%90 ehva na aelitefnidib cietneg aomittun
OCL A11 dan LCO 2A1
ucsea
s banlmaro lgaocnel ircog-iksnnsl avi a liegncy bsnsutuittio in eth lcorlegonpa elluemco "
hwhci nsame taht OI sah a iygcnel otistnuusitb adn rrehtofe sit naeblu to omfr a seondyrca tcrteuu.sur
uDe ot i'cneyslg smlal zsei, it tsercea sk"ikn" in the mniao acdi en.euscqe Teehs nksik ear deedne to cytlerroc rmfo hte dorsaecyn cuttes.urr
ehtOr swra:nse
XYG--yl is econbkba rof alcnloge pahal ani.hc 3 lloneacg paalh cnsiha aslipr to mofr rtplie lhxe.i yecinlG sha no R g,uopr lalwgoni rfo exiiyllbfit and ftiramono of elritp li.xeh No liycgne estevrnp this sicuotnuon lgps,aniri nnevpertig the ormniftoa fo gceolnal racdeonys .cutrrsetu
ellRca htta il-paeeslchha and htseb-saete era mpeesaxl fo csrayendo cuurt.ssetr sihT nca eb othught fo a fseiamonantti fo teh haapl .xheli
rNAehot way to egt at it is avi iinneol:aitm
A. hedrnyog dnognbi uondtlw leyrla gcaneh insec nehteir alenina onr niyglce era alo.B pr yGl &;tg aAl hutlo'dsn ghanec owh rplineo is oemiifdd I( amne it LC,OUD if hteer aws a crsite eindahncr ro tosnm,ihge tub tno a getar wnD)ae.sr nigthno ot atcinedi that llcgenoa eotdnigdaer is eldatre in sspereno to na AA stbt.utisonui o,slA in teh ontecxt fo OI c(hwih is hte inretepgns p,)liontcma ew ayleadr kwon htat the bemprlo t'esond ehav itnanhyg to od hwit eaer,diodgnt oemr tiwh het hagcne in ron. utEuctcsnrefut/i Hnoylste o'dnt on.wk
H’rese oen wya to psclitaooef-ne-semri eec“drdsea rbnynedod-hgo o:it”arfnom ’mI ont a bgi nfa fo ihst enil of a,nnigseor tub leyinctlahc lnneaia sa a dise rougp sah orme syre*donhg ofr onlaitept dhoegrny bgdionn hant giclney:
i:neanal HC3—
:cyilnge —H
,oS “lhe”,ciytancl naienal dlwuo tprmie mero drhy-bedonogn t,aomfionr chiwh mgtih wlola uoy to elmteinai htat hcoie.c
aTht iads, it seems omltsa bloisesipm to erul otu (thuwtoi ryev atnicehcl dkgenlwoe ro oesm eivddpro etpialxneerm aat)d htat het silglyth rrgeal eniaanl sdoe ont iipmar hergyodn bnindog teewneb onclgela olsmecule iav eitrcs al)(tpasi enetrreenfci. nI pliersm tesrm, neisc nieanal is elr,rga ouy lowud itnhk thta ti tums eswohmo trfnrieee whti het ebgdnnhin-dgyoor ahtt csrcou thiw hte yep-wdlit ceynlgi.
---
tSrit*cly ikens,apg it’s nto teh nrbmeu of yroengshd utb lsao teh tnrthsge of het olpdie thta ileatacifts gehynodr og:bindn a erhygnod nboud to a yngrslot nteteeeioagcvlr loemcelu elik roufniel ilwl p“a”rpae remo siovitpe nad, tsuh, doednbo-ghrny rome lgtorsyn hiwt a bnraye ngoxye oemracd(p ithw a yreonghd cctdoenen ot norc,ab rof maee.xp)l
hrFetru i:ngedra
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 timhg eb irkthenonivg it tb,u H nobd oamiotrnf of 'aas maesk eth rdnysoeac uurtesrtc of eth erotnip olanle(gc ni hist as)ec. eTh Gyl to aAl itbiutntouss sdeo lustre ni lsse H odnb ,aoomnitrf ubt fo livudadnii 'asa otn benewet nlleogac ecmsleoul (ttah gtmih eb erom ofr aatnrurqye tru)esurtc
rryaimP ctrrsetuu = mnoia dcai ecedsercauSnneqoy rtuutsecr = rrcsuutet fermod wthi a giesnl imoan aicd eseuceqn b(ate delptae stee,h ahpal xhel,i aetryit)ceT r rctsetruu = tllupmei nresdoyac uctterusrs neicargnitt erhegtto m(luptlie eatb edalpte teshse dtcaesk on otp of ceha rhote, rQceutrr ntaeay) rtcrtusue = nirteop ecuusttrr remodf fmor godlnif fo lla rtratyie rserctustu ot mkea ngniibd sste,i cet.
iecnS eth lanenia swa tup ni lacpe of het ,eniGcyl het pyrrmai rtctuerus swa blenua to mrof na halap hiexl eicsn hpaal eixlh esrsrtcuut deen a aulprtcira qsceunee (ylg - x- y) in drreo ot omrf ehyogdnr odsbn to peek het iexhl abst.el
htwa is oagecnll ? a ynaocsedr neortpi ru.stteucr
ehnw ouy oeervm genlic,y eht tmos buaandnt miona cadi , rofm the rcerurspo elmluoce lliw oyu get a oerppr nsoecdary rcusutetr ? ON
yGl si p,orla lAneian si aronlpon nad rhbydiocpho. Miseness nrncaoenevtosiv tnaiumt.o eeThs AAs veah eediffntr hmacicle pirosteper wchih aled ot esruitddp ioprten ongifld on(raycsde tuuesct)rr. arliimS ot uGl - alV noutststiibu ni ileckS lCle sDe.aise
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$279$49I inhtk it ahs gihotnsem ot od wthi ieynclg ue(d to tis mllas size it anc ift ni nmya lapesc hweer ohtre maino adsci can otn dna hcene ti dpersvio lctrta“ursu acotnc”mpsse ot teh n,llceaog ie.. tpu a inkk in eth plaah eh.lx)i If yngiecl si cpsildmae by mnioesgth eel,s I o’tdn knhti cr-lapngleoo can fomr tis otcrcer sdnocayre res.rucutt
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