I ir,duegf -g-ienYlcyX si ahcityellnc redcdesoni a yrpmra“i imona caid teutrcusr of a inreo”tp ncise hte inoentifid fo a rmriPya tsucturer of a tnoperi si a“ ralnei cihna of anoim i.cas”d fI yuo ssem twih het rPimary t,utcrsreu sa in hte siuteoqn ts,em ouy cnntoa orfm eth eydnaroSc tuecstrur of eth tenp,ior wchhi si niddetemer yb eht nbdynrone-oighdg ichwh cosruc ewbtene eth tpeidpe banobeck, nnedptnedie fo teh R orpgus. I ohpe isth emda s.seen
orFm edaikipiw: dnr“cySaeo ttueusrcr is llfyrmoa nededfi yb het teatprn fo ydrenhog odsnb tenebwe eth omain ghrdeyno adn yxrlboca yexong tmaos in eth idpeetp ancboebk”. hipesas(m )mnei
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.
ko ysug nda i teoqu romf /s.gdtoets.:harsi/el1pice/olopeweretias-i0wettcu/notmwo4sr/sbm2pfhtc
0"9% eahv na edtafienbiil cnteeig mttaonui L
CO 11A dna LOC A12
asu
sec baorlanm nagocell iigkocslnsnr- iav a ygnecli notttsuibsiu in eth callnpgroeo ullomece "
iwchh msean thta OI hsa a lneygic tousbiitustn dna eroehrft ist nbeual ot fomr a ecdasnroy eutcurrt.su
euD to snc'lgyei mlsla zse,i it etercsa s""kkin in the aionm icad suqc.enee heseT sikkn era eedend to yloccerrt morf teh rcasednyo rtsruuct.e
rhOte nsre:aws
l--XyYG is enkobabc fro longclae halpa .nciha 3 allconge ahalp hasnic asrpil to rfmo eitplr iex.hl elGncyi has on R gr,puo wlgonial ofr yliliitbexf dna ntmrofaoi of ptlrie ilex.h No nilgcye evspentr htsi soitoncnuu ign,lipasr vneigrtnep hte mftonairo fo lgeolnca syrenaodc tcuu.srrte
allecR ahtt llcahhpeae-is dna -btsaseehte rea mapxlees fo dnoecsyra sure.ruttcs iThs acn eb huottgh fo a tfmaaieiosnnt of eht lahap ilhxe.
NoertAh way ot etg ta it si iva mi:tolainine
A. hndoergy bdngino otwlund ralely necagh eiscn hireent aalnine ron niylecg era .Bor lpa yGl > laA houl'stnd hnecag hwo nreiolp si dmefioid (I amne it LD,UOC fi rhtee swa a tirsce hendcarin ro iosmgenh,t tub ont a tgaer wnDsaer.) ntnhgoi ot nteciiad ttha anecglol ndadoirgeet si etareld ni osenesrp to an AA utiosni.ttsub ls,oA in eht toxentc of OI wh(cih si hte esegtpinrn cinmltp)o,a we eaadrly oknw hatt eht pbemrlo 'tesndo aehv aghnnyti to do ihtw ddarentgo,ie mero tiwh hte nagche ni /cttcunerf r.iuuEtosn Hnsoyelt dton' kow.n
’Heres eno yaw ot -efe-iosmaltncipreos “rdseceaed rnyd-bdgeonoh tmronfa”i:o Im’ not a ibg fna of shti ienl of ,noiasrneg btu neyhacltcil aaennli sa a sied puogr hsa orem *neydgsrho fro aetotlnip hdgynero igdnnbo nhta nelgiyc:
ilaeann: C3—H
eyngil:c —H
,oS lle“”citnaych, anenlia lwduo miptre rome hdb-yoengdonr ,oorimtanf hiwch githm oawll uoy ot elimietan atht e.coihc
htaT sd,ia it esems salmot iemsolbsip ot rlue uot u(otiwht yrve ahnieltcc edognlewk ro some vdiedrpo peeernxitalm tada) atht the ihstlylg eagrlr ialenna seod ton pmiair ordyhnge binndog enewebt lencoagl oemlclues avi sietrc i)l(aatps tneciene.refr In peisrlm ,metrs nseci lineaan si r,egarl you wuodl ihtnk atht ti umst oomshwe reeetinfr hitw het onn-egdinrbhoygd ahtt ocrusc hwti the d-telypwi yencilg.
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*ytiSlctr apns,gike ’its ton teh neumrb fo nrgedhsyo utb laso teh rhgsettn fo the ielpdo ttah alateticsif hrgonyde inbdgn:o a rohgdyne undbo to a glyosntr ginaeeevetcrotl oemucell lkie elionfru lilw repap“”a omre opeviits an,d stu,h degdoonrybhn- remo ognystlr whit a eybarn gxyeon ropamc(ed ihtw a orhgdnye eccdtonen ot can,bor rfo ).exelpma
thuFrre gndare:i
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 thigm be tekvogirnihn ti but, H odnb onoifmrta fo aa's kasem teh secoadrny csrueutrt fo the inrtepo ngclle(ao in ihts ase.c) The ylG ot laA sbsuiuotttni dsoe utelrs ni ssle H ndbo nia,ofromt tub of daliivdnui 'saa tno tbenewe lacoglen esumlolec t(tha hmigt eb orme rfo uaanrtrqey ctur)ertsu
iayPmrr tuetrucrs = moina icda ne qeonucredyaSces tscutrreu = ucturrets mdfore iwht a egsnil imoan idac eeensqcu ate(b pteldae eshet, lpaha x,ihle irerTtecyta) utursectr = utimlpel oecdsrayn utserurcts irgaitnetnc hogreett pit(mulel beat delptae ssehet tkeacds no top of ecah hrto,e rcttn)uyeQ earar esrturuct = eoirtpn uctrrestu ordmfe orfm onfdgil fo lla trirteya rtrsutcues to maek ngnbidi iets,s tec.
Secni the nilneaa wsa ptu ni lepca of het cieG,ynl hte mpyairr ttuceusrr aws uanbel to orfm an lapha ilhxe sceni laahp ixelh tesrsucrtu ende a taclpurrai eesnueqc g(ly - -x y) ni rreod ot mfor onydehgr nbsod ot epek eht eixhl eltbas.
twah si cglenaol ? a aesorncyd enrpoti st.ucrurte
nhwe oyu rvoeem cg,lynie het osmt tdaunanb niaom idca , ofrm eht opuerrrcs melueclo illw uyo get a rerppo donsyacer rutustcre ? NO
Gyl is loa,rp enAilan is oaoplnrn dna d.ricpohbyoh isnsMsee ntenavrooinescv n.ottiuam heeTs AsA ahev rdefieftn ahlemcci rrpeeostip hcihw lead to udditrsep rtiepon odifgln ry(adcseno rustrutc).e rmailSi to luG - lVa tstuitubison in ilcekS leCl esasiDe.
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$279$49I ktinh it hsa itsneomhg ot od thwi lyeignc ed(u ot sit lslam izse ti nca tif ni mayn aecslp erewh horet oanmi acisd nac otn and cehne ti vredospi lrautcrs“ut mn”ccsaoepst to eth g,llacneo e..i utp a nkik ni hte hpaal ixlh.)e fI lnygiec si asempilcd by gmsnothei see,l I dnto’ ntkhi aopl-rncoelg nca fmro ist teorccr radecoysn suruetr.tc
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