I dfeu,igr iy-XcYg-nel is elahtncclyi drdcienose a yrampri“ oimna aidc rrtcestuu of a ”toerpni seicn het edonifntii fo a yrriaPm stcuturer fo a ortepni is “a arieln cinha of moain .adcsi” If yuo mess whit eth iyrmaPr rusr,tcteu as in teh oesitnuq te,ms oyu acontn frmo eth dyaeSncro seurutctr fo eht optir,en whihc is mednrtieed by eth godrn-iybgoednnh chiwh rscocu netewbe the tpepeid ekoacnbb, netdeinpedn of eht R rpous.g I ohpe shti edma e.esns
oFrm epiiwdaik: d“oarycneS rtctusreu si orllmayf nidedfe by eth apntret of rnedygoh donsb enetebw teh maoni odyrngeh nad bxrlacyo neyxgo smota ni hte eptdeip obnkecab”. (shsaipem )inem
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 gysu dna i otque ofrm osoe/datmpo-wtgl.n2/:weetceutlcpr/rsmihis4.poewa0tbi1she//oetrfscsit
09%" vahe na tinbaleedfii tingeec ntotaumi CL
O 1A1 nda CLO 21A
usaesc mrlonaba eoglacnl gsocl-isniknr iav a eilgycn btsiosttiunu ni hte agllenoorpc ocellume "
hciwh sname ttah OI ahs a enigycl ttntuoisuibs nad rreetfho tsi ulneba to morf a rseyadocn uretusur.tc
euD ot cesg'niyl lasml ,izse it eetrsca "k"snki in het ianmo cadi usqne.ece heesT kikns rea dendee to cyerlortc ofmr eht ncasodyer uttesc.rur
rtOeh newr:ssa
Y-ylG-X si cenbkabo fro econllga aalhp hac.ni 3 lcenoagl lhapa hnaics pislar to frmo rtlpie ieh.xl nyGceli ash no R uorpg, liawongl rfo llyeibxifit and imnoofatr of tleipr hle.xi oN inleygc etrnvsep hits nncousoiut nps,alrgii erngivnpte the tnafirmoo fo lcnaeolg dcoernysa .utsrcuetr
lleRac htat pea-chhlilsea nad seets-tbhae aer apeelmsx fo conesrday sr.eutstcur isTh nca be tugthoh of a ntofenasitiam of the alpah ilh.xe
rheNtAo ayw to etg at it si vai i:neltnimioa
.A ohergdny ndbngio ltodwun realyl cengha censi nertehi ninleaa nro iyclgen ear o.l rpBa lyG ;&tg Ala udsn'thlo ganhec woh ileprno is dfiemoid I( aenm ti OU,LDC if rtehe asw a eicsrt dahnircen ro mineo,shtg btu ton a ratge w .D)snera githonn to aeitncid ahtt aoeglcln dodteriegna si ledraet ni rseonsep to na AA ibtosstn.uuit lA,so in teh xentcto of OI hiwhc( is teh netnrgspie lcpon)ita,m ew ylardae wnok htat eth beoprml tn'sode vhea hatgnyni ot do ithw ng,raetioded oemr tiwh teh hcgean ni coruuit/.rEn utnetcsf ynleostH do'tn wokn.
’eesHr oen ywa ot imoosrpcetif--eeasln dedar“esce ben-ondygrdho otnm”rfo:ia m’I otn a bgi nfa fo tish einl fo seiaong,rn but yctlnacilhe lnnieaa as a iesd rugop has emor srenoy*hgd rfo lpnetiota eryondgh dgoninb tahn lignyec:
ln:aeani —C3H
lnic:yeg —H
,oS h“inyaclc”,tel anliane owlud ptiemr roem odby-hgonrdne oa,mrfotni ihhcw mghti aolwl yuo to aeimtlein ttah .heicco
That asid, ti seems latosm eliisbmops ot uler tou htotw(iu evyr claitehnc edkolwegn or seom vpodired erexeanlitpm ad)ta ttah teh tllyhsig rgrela ninlaea sdeo ont iarimp rygendho ionbdgn weteneb loleagcn eeolumlsc iav stcire )aplaits( f.eetrieencnr In ierlpsm ,ermts secni lniaane is rlra,ge ouy douwl htkin tath it tusm emwohso eeeirrtnf wiht eht horoynnengddbgi- hatt crscou tihw eht piy-teldw ycelngi.
---
rci*tltyS gps,aiken i’ts not eth uenrbm of goerydhsn btu oasl teh hnesgrtt fo hte ledipo hatt italcetfisa dneogryh gdnbon:i a yronedhg duonb to a sroynglt necetlvagoirtee elmulceo keli nrieolfu wlil pepa”r“a eorm siviopte a,nd hs,ut e-gdnohdrbyon oemr slygnrot twhi a nbaery gnyxoe (ermocpda htiw a rgedynho cetndenoc ot ncr,boa for ma.lxepe)
ertruFh gria:nde
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 mithg eb knhtirviogne ti bu,t H obnd oftnaromi of aa's eakms teh snyrcdoea tutsrurce fo hte nproite olg(lcaen ni isht ce.sa) eTh ylG to aAl titnitssbouu sedo estlur in lses H obdn fnaroomi,t tub fo vidinliuda aa's not bteewen gaconell ecsllmoeu (ahtt imght be moer for atyuaneqrr ucut)trres
miyPrar uusrectrt = oainm caid n eynaquceroSescde sueuttcrr = tsrruteuc oefmdr thiw a ilnges aomin cdia equneesc btea( edtpael hete,s lapah exi,lh tcryar)ete iT ttucuresr = mtepliul dornscaey uurtctsser cinrtigtena thoreteg lemiltpu( taeb detelpa setesh ctsdkea on top fo chea ,tehor ectryrt aaQruen) sctutreru = neporti eucrtstur ormdfe rfmo fndiglo fo lla erttirya srruetsutc to ekam ingnibd s,iset t.ce
cieSn the aiaelnn swa put in clpae of het eyGil,nc eth pirarym cretruust swa lnubea to rmof an apahl hliex secni aaplh hliex resrtusctu ndee a utrraipacl eecnsqeu lgy( - x- )y in oerrd ot from ydegrhno dobns ot ekpe hte xelhi besla.t
htaw is llgoenac ? a erysdanco iteponr utturc.esr
hnwe yuo eemrvo ,geciynl the mtos ananbtud aniom idac , mrof teh reurprcso eeocmllu ilwl oyu egt a ppoerr ndyeacsor seruutrtc ? ON
lGy is ,aoplr annlieA si aonnoplr adn co.yhrhpobdi sienMses teoarnvicvesonn u.oitnmta Tehse AAs veah rnetediff cmiacelh epstierrpo cihwh eadl to dpseidutr eopnitr oindlgf (nacedyros sc.u)ettrru iaSrmli ot lGu - alV utsboitnuist ni eSlcki lCel Diae.sse
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$279$49I hnitk it ahs tnighosem ot od wtih iecyngl (due ot tsi mslla zies ti acn tif in aymn aeplsc rhewe roteh nmaoi dasic can not and neehc it rdioveps ucartr“lsut psse”ccmnato to the nlgoecal, .ie. upt a inkk in hte halpa x)e.ilh fI gleyicn is sidpamlce by inhtsmgeo s,lee I n’tdo khitn -rloglnaepoc nac fomr sti rcteorc roesdcyna uur.setrtc
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