I grdufe,i -inXgYecly- is niyhlceclta ernidodesc a rp“mrayi oamni icad urtescrut of a ritopn”e cesni teh fdnntioiei of a Piryram erutuctsr fo a rtenpoi si a“ rleian anhic fo nimoa isad.”c fI uoy emss wthi hte riaPmyr urtscte,ur sa in hte stqiueno ,tsem uyo ntoacn romf eth eordcnSya eturctsur of hte e,noprti wichh is dinemtrdee yb the bnionrd-hygdgoen hchiw socurc beeewnt eth etepidp nabbekoc, dineepnntde of eht R .rouspg I hope stih aedm sees.n
moFr waiedikpi: ancr“Sdeyo tcursretu is fmraoyll ndidefe yb eht trpaten fo hoyrnged odbns bteenwe the noami nhrdyoeg adn yxrclabo yxnoeg soamt in teh edeitpp bbnkcoae.” ha(espsmi i)mne
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 ugys and i queot form 1b-dmshw0t4/wns:/siea.ofusspmwrhle/ecipeo/le2tsrit.igoetttcooetr/apc
0"%9 ehva na iaitibedlnfe giecnte ttnmiuoa CL
O 11A adn CLO A21
uscsae blnroaam calonegl icg-solrnsnki aiv a yneigcl uiitsnstobut in teh anllpecogor omcellue "
chhwi amsen taht OI ash a yelincg onutstutisib dan otrherfe sit anbeul to morf a dascoenyr r.tsuctueru
euD to n'ecyilgs malsl e,isz ti atecsre "kikns" in the nioam caid seqeeunc. hseeT ksnik are denede ot eyrotclcr fmor het necdaryos rcsre.tutu
Oerth wasrsen:
--GXYly si bonebkac fro ealnclgo phlaa ianhc. 3 ecgollna hapal sahcin raslip ot romf reitpl .ehlix Gnyeilc ahs no R urpog, gnwilalo fro bfxieilitly nad tfmnrooai fo telrpi i.xlhe oN nlgeciy pntseerv htis tunuicnoos gpn,sliria vgetipnern eht oiftomarn of loclngae yaesocndr rusrt.ceut
lalecR that laaheehlcs-pi nda hstta-eeseb rea apexlems fo orscaedny ctrutessru. hsiT acn eb ghuhott fo a iomnfintasate of the hplaa lei.hx
AeNotrh way to egt ta it is aiv o:ailnnetimi
A. ynoeghdr bnodnig utdnowl aellry hgneac nesic heitnre aanlien ron cienlgy rae pa.l roB yGl ;t&g lAa 'tdohlnsu ehgnca ohw neploir is fieioddm I( nmae ti LCUDO, fi tereh saw a scetir hrndineac or mt,hoseign utb nto a rgtea w.es )nDar tihnngo to ecitanid atth lngocela dentoergdai is rdtaele ni sepenosr ot an AA tstboiituuns. Alos, in teh cttneox of OI (wcihh si the tnrsipegen )om,nlcitpa ew elyarad wonk atht the elompbr sntode' ehav yignnhta to od hwit gto,endediar emor wthi the hcgaen ni tfnu rc/teus.nruoEitc tsnoelyH ton'd o.nkw
see’rH one ywa ot sifmrceneilepoa-t-os erdesec“da debgd-yoonrnh anmf”i:otor mI’ not a bgi fan of thsi inel fo na,sognire utb ylteinalhcc inaelna sa a esdi gropu ash mero rg*eysnhdo fro oetnlpiat gnhodyre odbnngi ntah lncyieg:
nalien:a H—3C
nliygec: —H
,So lynal“tcch,i”e leaiann udwlo mptrie orem nrhydoeog-dnb onamitofr, whhci imthg waoll yuo to imlteaein atht ic.heoc
Ttah ,dasi ti esmes maslot biipsomsel ot elur tuo ot(ithwu yevr iecltcnha ldeeowgnk ro smoe pvdriode eatirnmpelex )data tath eht lhtlgsyi gaerrl nenalai oesd otn iaprim eghronyd nbgnoid etewebn lnlgoeca sclulmeeo vai irtesc )aasptl(i e.etfnecrenri nI pseirlm rsem,t escin laaienn is ,gerlar oyu lduow khitn htta ti tsum omwohse rfinetree htiw het o-hndryngigbdneo atht ucrocs ithw eht dle-wpyti ynlegci.
---
*ttryilSc kpeg,aisn ’ist ton eht berumn fo ednsogryh tbu olas the trnegsth of teh iloepd htat iafacseltti yregodhn bi:ongnd a ynrgohde obudn to a tlogsnyr ioeegaetrecnltv lucemoel ikel fneiulro wlli epap“r”a rome vepiotsi na,d st,hu hrdgny-odneob mreo ylrsotgn hitw a erbyna nxogye (ocmaedrp thiw a ehdoyrgn ectdnnoce ot nc,obra rof .aeple)mx
theurrF nriaed:g
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 igthm eb khveiigrotnn ti btu, H dnob otomirnfa of 'saa esmak het noysardec rettuusrc of the riotpne gec(lolan in shti esa.c) Teh Gly to lAa tutbtnsiiuso oesd sutlre in elss H obdn aitofomn,r btu fo liiudvnaid saa' not enebtwe llocgaen oleesuclm (htta gmhti eb oemr fro trryaqenua ur)ttsecur
mrryiaP uusctrret = amino aidc ocryns enqueeaecdS urtrucest = uturcsert roefdm thiw a geslni imano dcia eesqnuec (beat dltpeae tsh,ee pahal xhiel, trri)eytcTea crersuutt = ltpleumi andrsyeco uttuecssrr rinctategin egerotth l(iplumte eatb edapelt sehtes stcaedk no tpo of echa ,throe ct aaQryn)rertue trtcurseu = nprtoei rtuerstcu oemdfr fomr oglfdin fo lal treiyart esrruttscu ot make nidingb siste, t.ec
nicSe hte leanian aws tpu ni leacp fo the nli,yceG het mirrapy rcttruuse saw uablne to fomr na hlpaa ehlxi esnci lapah xheli ueustrcrts eedn a caaptrirul ucqesnee gly( - -x y) in oedrr ot fmor nogdyerh dnbos ot eekp het lxieh slbte.a
twah is gallncoe ? a nsyeacord oinpret utcurtesr.
enhw yuo omevre n,lyegci eth msot natnbuad imnoa idac , from eth rceprrsou uoellmce llwi ouy get a poeprr ydcranseo tcsuruetr ? ON
lGy is aop,rl nlniAae si olnpanro nda hydoibhpo.rc eMsnesis osaitnrovnevcen matiu.ont eeThs AAs vhea dfferient cliemcha sreppreoit ihwhc edla to drtdsiepu noetrip odlgnif aocnres(dy ctet)rsu.ur Smaiilr to lGu - aVl osttitusinbu in liScke lCel aDs.iees
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$279$49I hntik ti sha iomshegtn ot od wtih yleingc ued( to sti lalsm zesi ti cna itf ni yman clspae erweh hrtoe nomia adcsi acn tno nda ceneh it pesrviod “ttalcrsruu pacso”cments ot teh nglc,ealo .ie. tup a knki ni eht hplaa hxei)l. If ylecnig si paeicslmd by hitesnogm sle,e I ’notd ihtkn lecglapo-nor nac frmo its rtorecc orcyedasn u.crttsuer
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