I gdiur,fe ncYXig-e-yl is llctcyiehna oisrcdeedn a pary“rim anoim dcai ecrrutust fo a eoprti”n nscie eht idoniientf fo a airyrPm uurtrtcse fo a ptrenoi is “a lniear hncai fo miano siad.”c fI ouy mses thwi eht iPaymrr rsrt,uteuc sa ni teh tusioeqn tms,e yuo cnotna from eht acSrodney cuttesurr of teh poteirn, ihwhc is netedmdier yb eht ogiynnndgrd-beoh hhwic crsuoc betnewe eht dpteiep benabkco, inntnpedeed fo teh R og.psru I peho itsh adem e.sens
rFmo iwkeapidi: “Saecdoryn sruucettr is ylfmoral nieddef by eht ntretpa of ehdoynrg sobdn etbeewn eht aomni dyhorneg nda ryxolacb xngeoy atsmo ni hte iptedep beanbcok”. isps(amhe nie)m
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 gyus nda i oquet ormf otaeuhwsw/-:rget1ps/ioimfrcpbe.m/trcst0oa4h/wtsps2ld/osc.teeeetnoiil
"%09 aveh an idinlbfeitea tgceine tnmioatu L
OC A11 dan COL 2A1
easscu rmbnaalo goalecln -nsscliorkign vai a cngyiel snbtstutiiou ni hte lcgoreonpal uleecoml "
ihwhc maesn that IO sha a gcleyin nituibtssuto nda rhroftee sit ablnue to ormf a esdrnyoac t.uuutsrrce
Deu to yni'lgesc lmsal es,iz ti asetcre n"kk"is in eth mnoai cdia enuq.sece sehTe sikkn ear ddneee ot ltrcyorec ofrm eth csyonarde .uurtcters
htreO rane:wss
-GXyl-Y is bkaocbne orf cloagnle pahal cain.h 3 ogelclan plhaa niscah paisrl to form trilep .ixleh cGinlye ahs on R g,pruo laiwongl fro eilxyilfbit nad miafonrot fo lirtep lxihe. oN nlcyegi epvetrns htsi nsoutuconi lrnias,pgi gpetninrve het nfrtiomao of geclanlo ondsyearc rreucts.ut
Relcal htat hpseli-haeacl adn hessetaebt- rae xepsmlae fo radsyneoc .suectrtusr siTh cna eb ghtouht of a sntioimtafena of the phaal elh.ix
teNoAhr ayw to etg at ti si aiv aoiii:mlnent
A. ordnghey nidnbgo otdunwl relyla hgnace necis rtieenh ilanane ron iyegcln rae Br.p loa yGl ;&tg Ala houln'dst nhgeca hwo lrpione is fidmieod I( naem ti ODLU,C fi ethre wsa a sritce anredhinc or hsitegmo,n tub ont a etgra .sDwane )r tngionh to ieincatd htat lnlcoaeg otdnareidge is earetdl in sseepnro to na AA .tsiinbusttou ,Asol in eht xnttoce of OI hc(wih is het gptensnrei oal)c,nmtpi we ldeaary know atht het bmelopr ndeso't heva nniyagth to do ihwt iedgntor,dea oemr thwi eht hgncae ni en./iunu uEotfscctrrt Hneytlso n'odt .oknw
H’sree eon yaw ot elimf-rcepoot-sainse reed“aceds gebyo-rdhodnn m:nto”orfia ’mI otn a bgi afn of htis niel of grnan,ieos btu liycelctnha aelnain sa a idse pugro sah moer snoryg*ehd rfo elitatnpo ndehrygo onigbnd ahnt ilcengy:
aneail:n C3H—
n:cyielg H—
,So hcntaiyl“”e,lc elnania wluod rptime eorm hdogbyendnor- af,ionrmot hhwic ihmgt wlalo oyu to eleniimta taht cie.ohc
Ttah disa, it sseme tmlaso mbioeslpsi to elur otu hwt(uoit rvye laicnehtc lgkoeenwd or esom dordviep rlpeenmetixa )taad thta teh hysiltgl rlarge eaialnn dose ton ipiamr dhgyenro ibngdon ebneewt ngcealol oumslceel avi stceri lait)as(p eneretrc.nfei In rsepmil es,tmr ecins leianan si ,regalr yuo luwod hitkn taht ti must hoswmoe iftreenre twhi teh h-gdeonydnogrbni tath uocscr itwh teh ptyed-lwi gncliye.
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ryltiSt*c ikangps,e ti’s otn the emrubn of erhndygso utb osla the rsghntet fo hte oidlpe ahtt slctaaiefti ynrohdge ngdbo:ni a eydorgnh bnudo ot a trsgolyn atglornieecveet omluelce ilek nrufielo will rp”epa“a omer itvepois ad,n ,sthu ohbogrdye-dnn rmoe lynogrst twih a nbeyra xegoyn madc(orpe twhi a hodyrgne nndeceoct to onrbac, ofr aeexl.mp)
rtFruhe girnea:d
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 ghmit be ietgrkvhnino it ,but H bdno iafmrtnoo fo 'aas esakm teh yocesarnd tseructru of het ortinep aoenc(lgl ni hist easc.) ehT Gyl to laA soutitinbsut edso uetslr in lses H bndo ainm,otfro tub of dunviaiild 'saa tno eebnwte ocnlalge lluceosme ta(ht higtm eb meor rof reqynataru escrurtt)u
Prriaym rreutstcu = imano icda Sqrcnyecnaoesedue utrrtcuse = seurtutcr doemfr thiw a elsing maoin icad uesecenq ea(tb dptaeel eeh,st plaha xeihl, eTeryicatt r) crsruttue = eimpllut saoenrcyd etrcrstuus negiractitn gteohtre m(tpiulel aebt plaedet esetsh kcedsat on pot of aech ,etrho caerartynuer) tQ rttsrcueu = pioenrt suctturre oremdf mrof lnogfid of lal aytriert urtersstuc ot meak gniidbn ,tssei tce.
iecnS het lieaann asw tpu in ealpc fo hte cGl,ynie eht mayrrip cteurruts was anuleb to from na hlapa hliex nseci apahl heixl ecurststur ndee a rucpiatrla enseuecq ly(g - -x )y ni eodrr to morf rednohgy odnbs to epke eth heixl atb.sel
whta si goalnecl ? a eordsncya rtoenpi e.uutrcrst
wnhe uyo roeemv ,gnceyil the mtso anntabud ionam cadi , mrfo the rroeurscp ellocume lwil uyo teg a reorpp rycenaods cttrruues ? NO
lGy is oa,lpr enAilan si rlpaoonn nad ochh.iobyrdp sseeinsM oiecrnoevnvsant tinau.omt Tehse AAs have dfitefren limheacc seripreotp ichwh leda ot dreutpdsi peonrit olfingd do(nresayc sc.rurt)tue Siliarm ot Glu - Val tbittusinuso ni kiSelc Cell .seieDas
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$279$49I nhikt ti sha sigmoehnt to do tihw iclgeny u(de to tsi alsml siez ti nac ift ni many cpales erhwe rheto onima sidac nca ton and enceh it svdepiro arctusl“rut csmoptsec”an ot het lecnog,al .ie. tpu a ikkn ni eth lpaha ex).ilh fI ncegily is dclseipam by iehtmosng s,lee I otd’n kntih gerpc-lolona nac frmo tis torrecc eyrdasnco eturstucr.
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