I rudgfei, l-cXyeYing- is lycniehclta drcdnoiees a iyprr“am imona iacd srtuetcru fo a teniopr” iencs het odntieinfi fo a raymiPr ruttrescu of a oertipn is “a nleair hcnai fo namoi ”sacdi. fI ouy essm tihw the ryPirma ,tuerutscr sa in eth sneiuqto s,met ouy onantc omfr eht yracSndoe ectrrutsu of teh otpein,r ciwhh si mneededrit by eht ggnondnhr-idbeoy iwhch croscu eetnbew the depeitp eocnabkb, pednntiedne of het R grsu.op I oehp htsi amde e.nsse
Fomr kipwdiiae: dyeoS“cnra rrestucut si falyroml fiedend by het npttare fo ghrodney sdbno eewentb the aomin horygnde nad xolbyacr gyenox osamt in het etpedip aobbcnek”. m(ishpsae )enmi
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 sgyu nad i otueq ormf fwlcmrpoethltpgs/t/nrtow/op-i0icirt.ibt4mseho2sso1/scteae./eseeuwad:
"%90 aveh na flnibietiade eencitg naouttim
LOC A11 nad LCO A12
uss
ace ramolanb lealngoc oliksrncn-sgi avi a egcinyl tuonistbsiut ni teh cloprgonael comelelu "
cihwh seman htat IO ash a lcnegyi tosttbusunii nda toreherf tsi uelnba ot rmfo a nydcorsea uttruruce.s
uDe ot ygsin'cel slmal esiz, ti etacesr snik"k" in eth iamon caid ecuesn.eq esehT kikns era eedned to cyrrotcel frmo the radonycse ets.trcuru
tOreh ns:swaer
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llRace ahtt sleh-ahcaiple dna esat-hesbte era aeelxspm of rdaesyocn tuuect.srrs hsTi nca eb hogthtu of a aetnsinmoftia of the alhap x.lehi
hNrteAo yaw to gte ta ti is via iiei:lnanmto
.A gnyhedor bnngdoi noldtwu ryeall aceghn inecs nrieeth ienaaln nor iclengy era ol.rBpa lGy ;g&t lAa nshl'utdo ngahec who irnpole is ioedifmd I( nema ti ,DLUCO fi ehret saw a sciert dianrchen or gostiem,nh utb ton a tareg n)aeDr. ws nhtonig ot tiaecnid that lolceagn dogidteaern is teedarl ni esrposen to an AA n.utbiossiutt ,lsoA ni eth tnoxect fo IO whch(i si het gptnseneri c,pimlo)nat ew aaydelr oknw taht hte bplrome d'nsoet have taihnngy to od twih rotd,ndgiaee oemr with teh ecahng in tni/o uurfEnsrt.cuect etonHsyl todn' nwo.k
esHer’ noe awy ot clrt-pmanees-ioofsei edarsd“eec eryhgdonbodn- tomrinfa”:o I’m nto a ibg nfa fo ihst enli fo so,neanrgi tbu hlliccaynte nanliae as a side uogpr sah mero ed*nohgyrs ofr tonpaleti engohdyr oinngdb tanh ncyegli:
inlaean: —C3H
lc:nygie H—
oS, chlecily”an“t, liaeann dulow pitrem mreo nygdrbh-eodon fora,minto chhwi igthm laowl you to ialieemtn that e.cocih
Thta dsi,a it eesms ltamso osmliepbsi ot uerl uot wihottu( vyer nlcachtei kodnweelg ro soem ripdvoed eaimplxnreet data) atth the htslylig glarre naleani sdeo nto apiimr rgonydhe ndniobg etnwbee gnaeollc clolmuese avi ecirst (li)aspta ecit.feerrenn In milersp sem,rt nesic alnaine is el,garr yuo wudol tnihk thta it muts owmhose erenifter iwth hte dogorhnebdn-iyng taht surcoc twhi teh t-dwlpiey cilgeny.
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tilctSyr* ,pniesagk ts’i otn hte breumn fo redshoyng btu soal teh gethnsrt fo eth eodilp taht fcstitlaaei dyhgoenr :noibndg a heygdonr obdun to a sotyrlng ltienecgeroveat ueclolme ikle lunoierf ilwl aepap“”r eorm viptseio a,nd t,uhs hodgnbnodye-r orme srtlogyn ihwt a ayebnr xenyog racoep(dm htiw a yhregodn cceondnet to o,narcb fro xpaeml)e.
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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 thmig be ngiehniktovr ti ,tub H donb torifonam fo as'a ksmae eth ascrndoey rcutestru fo eht oertinp lnogle(ca ni hsit .ae)cs ehT lGy ot Ala tsuitnboitsu seod ltuesr in essl H dbon ,frtmoniao but fo dnaiiulivd asa' ton tneebew galcnelo moueclsel (ttha gmtih be emor orf yurtrqaaen )ustecrutr
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iencS eth naenlia saw utp in elcap of eth c,iGelyn eth raiymrp usuterrct wsa ulabne to fmor na alhap hxile secni aaphl lehix rtcussretu eend a alicraprtu seequnec yg(l - x- )y ni oderr ot fmro oydrhgne bsdno ot eepk the hlexi l.eatsb
ahtw si nceloalg ? a dnoryeacs retpnoi ruurcte.ts
newh uoy revmeo nygle,ic teh mtso annubatd naomi cida , ofrm hte opcreurrs uoelceml illw oyu get a pporre scoryande suctrruet ? ON
Gyl is aorp,l Alniean si aorlnnpo nad odhyhrb.iopc snisMsee oeivnnsroencatv ntt.imoau eehTs AAs eahv enifefdtr mchlciae orsiteperp iwchh dale ot tdspdueir eonirtp dlognfi rocnsdye(a t.ursre)uct lirSmai ot luG - Vla uositbnsttui in cSklei lelC siD.eeas
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$279$49I ktihn ti ahs oghetsnim to od itwh lngyeci ude( ot its mslla eisz ti cna fit ni amyn calesp hrwee oterh ionam scdai anc ton nda eench it ievprods tuutrrlsac“ cnatcpo”sesm ot hte agncolle, ..ie utp a nkki ni the hapla ex)hli. fI lyiegcn si msacielpd yb netmoighs esle, I n’tdo ikhtn ol-crpaonegl cna frmo tsi erocrct nyocsedra .eusrtturc
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