I dei,rugf Yyel-Xni-gc is ytcleinlahc eedrcnsoid a rp“aiymr onami acdi curturtse fo a ”tpnrioe ceins het onitdfinie of a yrmPria tuserruct of a peitron si a“ ilaenr inhac of niamo .”idacs fI uyo smse twhi hte ymrraPi tsceur,utr sa ni the niqseuot es,tm you ntocan ofrm eth cSroeadyn cretrtuus of hte r,tnpeio ichhw si ntidemerde by hte eh-dbongnrgiydon wichh rscuco etbewen teh epiepdt bnackboe, eidtednnpne of het R rpogus. I hpeo hits mdae e.enss
Fmor dwiaipiek: edc“onrySa uruscrtet si yolmalfr ifdeend by hte rpnttae fo ngyeorhd bsnod teewbne teh omina egnorhdy and loxabycr yxeogn otsam ni hte ietdpep knebobac.” iamseph(s i)emn
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 guys nad i outqe ofmr ila.e:imtre/hosrapsifttnhw.c/c4-estgswbuld/stc0eieo2tretp1s/e/ooowmp
"0%9 veha an eblniidfetai nigecet titaunom C
OL 1A1 dan COL 1A2
acses
u rlbnaoam eglocanl igkninlcsrs-o vai a icnyelg uitsobiuntts in hte llorpaoceng ocemleul "
whchi naems atth IO has a egcyiln isuttunobtsi and etofrreh sti leuban ot mrof a nerayodsc cu.esruuttr
uDe ot cneigys'l alslm zse,i ti asteecr i"ks"nk in teh imnoa cdai ueee.scnq seTeh ikksn aer ededne ot letcoryrc fmor the reoncdsya st.utcerru
hOert eswas:nr
y--lXYG si eoakbcbn rfo llegnaco ahlap ciah.n 3 glcaenlo phlaa ianhsc praisl ot rmfo tprlie x.lehi clneyGi has on R gu,por ilwlngoa fro itxyillfebi and ontoafmri fo lepitr hle.xi oN ncyelgi etsvrpen tihs otnnouucsi irngisapl, rennevtipg teh irfnooamt of caoglnel ydasencor cs.ertruut
ealRlc tath ihalepecl-ash nad tateb-esshe era lxpseame of oecnardsy r.usucsetrt ishT anc eb tgtuohh of a aastenitmifon of hte palah e.hlix
rthANoe ayw ot get ta it is aiv :annitomiiel
.A ynedrgho bignndo tundowl elryal chgena esnci tineerh ainaeln nro cilgyne rae orl.paB ylG gt&; laA nusd'hlto cahneg how lnireop si oimefddi I( enam ti CUL,DO fi ether asw a itrsce enncihadr or omtg,ehnis ubt ton a rteag wre.a Ds)n nogtinh to etadcnii htat eloclnga edonedtgrai si detelar in erpsneso ot an AA stttib.unsoiu Ao,ls in eth ttcenox fo OI whh(ci is het nnesrtgpie ,nm)pcliota we aaldrey nokw atth the rempobl odetn's aevh ianyghnt to od whit tr,dodneiage emro whti teh enahgc ni rttc/ns efnEi.uuocrut nltoesyH 'ntdo kn.ow
sH’ere oen awy to s-ilerofpcetmens-oai crsdeaeed“ -rehngodbndyo n:am”oiotfr mI’ otn a big fan of ihts niel fo ,aoignrnes tub yaichelcltn alnaien as a idse ropug sah mero onr*yshgde fro ilontptea drynhgeo gibondn naht yceilgn:
n:nealai H3—C
egny:lci —H
,So nch”“iallecy,t inaenla wdoul itmrpe orme rndnegobd-oyh rootafmni, hcihw hgimt aowll oyu to ieaelitnm htta .ihcceo
tTah d,isa ti emsse omltas slbipmesoi ot erlu tou i(ttwouh rvye cahliecnt kdeognwle ro msoe ioddrvep pialetxrmnee aadt) ahtt eht ghlilyst elagrr nanelia sdoe ont irpiam egodnhyr odinbgn nbwteee anegollc emlluceos via ctrsie pila()ats enfn.reeeicrt nI rpelsmi restm, siecn inenala is ,rlager uoy udwol nhkit htta it tsmu oehswmo inreteerf ihwt het edngon-idhrbogny ttah cscuro tihw eht wildeyt-p ygencli.
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c*ylrtiSt ,spiangke s’it ont het rumben fo ohdesngyr ubt alos teh tnehstrg fo teh loiedp that ateiictalfs doynhrge ng:ondib a reghnyod oundb ot a rgnsyolt eatirevlotgncee mecelulo iekl firnelou iwll rpap“”ea oerm tpoviesi and, ust,h oeghrbodnnd-y ermo ngrtloys itwh a eabyrn ygonex od(cparme hwit a hdrogeyn ecdcenton ot brocna, orf e)pxlma.e
ehrFrtu rdnaig:e
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 gmiht eb nviitgrkohen ti ,but H nbod itomranfo of 'aas meska the radnocsey tsureutrc fo eth roenpit l(noelgca ni tish c.s)ea The lGy ot alA uitstuniobts eods retuls ni sles H nodb ofrmot,nai btu of liinvaduid aas' tno twbenee colganel smlueoecl hta(t ihgtm be moer for yatrruqane ruust)rtce
iayrmPr trtcesuur = inmao diac oe Sedunraeqceycsn ertutucrs = urtescrtu dfomer itwh a ilgnes aomin idca encsquee eb(ta eeatdlp hste,e lphaa hi,lex taTe rerytci) rustreuct = llueimtp ocdsyerna urcstruest nittgriance eegothrt mtipe(ull tbea lpatdee ehtess kadcste no top of ecah e,hrot cyraeaQterr un)t ttsuurrce = iotnpre crursetut dofrme mrof nodlfgi of lla yatetrri ucurstetsr ot make ibdingn esi,ts tce.
ceSin eht lneaani swa tpu in clape fo het yil,ecnG eth ymrripa uretutcrs swa ualneb to frmo an lhaap exihl sncei hlpaa hxiel trsutucrse eden a palrctruia seeuneqc (gly - x- y) ni deorr ot rofm eoydrhgn sonbd ot peke het ielxh l.stabe
wtha si lecagonl ? a yrnseadco nrtepoi sue.rructt
wehn oyu mevoer lnyci,eg the smto badtanun nomai iacd , frmo het urpcroser omelluec lliw ouy egt a rpreop odryaencs rutrtcesu ? NO
yGl si paorl, lennaAi is roolnapn dna biochdhpy.or sMensesi itavnsneecronov attuom.ni sheeT AsA vhae efieftndr cilceamh reisrotppe hcihw elad to rdiedstpu prteoin lniogdf dearycns(o .sett)cuurr lSmiari ot uGl - lVa itbntouutsis ni kliSce leCl eesaDi.s
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$279$49I nhkit it has ienmosght to od iwth enicylg e(ud ot ist mllsa ezsi it nca ift in ynam espcal ehwre rteoh amnio isadc nac ont adn eench ti pesviord csarutu“tlr csmcs”peoant ot eth ncglel,ao ..ie utp a inkk in het aplah ).xleih If glcneiy is iamlecsdp yb nsmtghoie ,eels I ’odnt inhkt nglaec-rloop cna ofmr sit ctecrro ansedcoyr tcturseru.
$279$49