I fuidrg,e lX-g-icyneY is yltlceicanh nrodeesidc a ipry“amr onima icad eturrucst fo a i”etporn scnei hte tdnnfiiioe of a Pyamrri uercsuttr of a pineotr is a“ ilenar iacnh of noiam ”si.dac fI ouy ssme hitw the yPamirr s,etctrruu as in het einqstuo ,tems uyo nancto mofr eht rcodneyaS rtucsreut fo hte inpte,or iwhch is mnderteide by hte gndnegnir-doohby hhiwc uocsrc tbwneee hte ptepide banebcko, epenednndit fo eth R gurp.os I oeph shit edma seens.
romF akwiiedip: eroSdcnay“ esturctru si mloalrfy eeinfdd by eht rtepatn of gorydenh bnsod nbwetee hte aniom ynegdohr nda ayolbxrc geonxy osamt ni hte peptedi naebokcb.” sphmiesa( neim)
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 sygu nda i teouq morf lhtgbhes:.lo/-4foeeapio/dcs0iiw2tspwoer.atttmtpicrsm1es/nureecoswt//
"%90 eavh an iibtfnleiead ecgietn inotamut
COL A11 and COL A12
esausc
arblmano loealngc nrlsicgks-ion vai a iclgnye itubsnstoiut in eth gapoorlelcn emlelouc "
cihwh esnma htat IO sah a ygilecn utsbiotuisnt adn erefthro ist elbnau ot rmfo a rancoseyd cuus.turret
Deu to cesiynl'g lslma zse,i ti acsetre nk"k"si ni het mnioa dica sen.cueeq These nkski rae eednde ot ltecyrocr mrof het deoynascr tsrtuuc.er
trhOe wnsar:es
--yYXlG is banboekc orf elnaolcg phaal nc.iah 3 lloecang aalph ansich lsprai ot rfom trleip x.ileh lyecinG ahs on R pgrou, lgnliowa orf efyiblltiix dna ionartmof of plreti lie.xh oN yinclge prevesnt iths uutoicsnon ars,lgiipn nneietrgpv teh oiomanrft fo laclgoen nacdyrseo u.rtceruts
clealR thta chhlpeaeslai- dna te-tashebse aer lpaxmsee of adsencyor trr.scutesu ishT can eb gthotuh of a msetitanifoan fo eth palah x.ilhe
oheNtAr way ot gte at ti si via ieliatmn:ion
A. nyrhodge ngnodib dotnwlu yelalr ehcnga ceins nhirtee nainlae nor cinelyg era Blar.op Gly t&g; Aal slndto'uh gahecn owh orelnip si efiidmod I( nema ti DO,UCL fi eetrh aws a sitrce cdnrnheai ro o,ntemgshi ubt otn a rtaeg nseaD w).r tgninho ot aedicnti ahtt olclaeng rgiodeendat si derlate ni eponsesr to an AA i.ussbutontti lsA,o in teh ntexcto fo OI (hihwc is the ienegtrpns nmt)ipcla,o we ldyreaa konw ahtt het bmlorep edots'n aehv nyhnitga to od whit eoddinrtega, mroe with eht aegnch in /crtfnttoircn.es uuEu nlHsyteo tndo' wn.ko
reesH’ one awy to eecrseooil-i-stfanpm adeserce“d ogyrodn-ebndh to”:nfarmoi ’Im not a gbi fan of hsti inel of oai,rsnnge btu caectillynh anielna as a isde pougr sha orme sod*nhgeyr orf pltienato orhndgye dnbnoig anht incgely:
eanialn: C—3H
l:yecing H—
S,o ectnc“halyi,l” nanleai lwuod mripet emro ogbdoynder-hn ,ofmraiotn hwhic gimht woall uyo ot ntemielia that eocich.
athT si,ad it seesm smtaol elbspoimis to uerl uto twtui(ho very htecailcn delwnokeg or esom dpveodri nitmeraelxpe adat) ttah hte shyigllt eglrra leaanni dseo otn pamiir ghryedon nndobgi newebet eglonalc eelsclmou via sertic t(asa)pil etr.nreienfce In limsper rm,ets icsne lieanan is egrla,r ouy oduwl nktih ttha ti stum ohwemos efeernrti ihtw teh eighybdnr-noongd atth scocur twhi the pd-yliwte igyncel.
---
*iyrtSclt ksn,peaig ’its nto het rbuenm of heoynrgds tbu soal hte thtsgner fo eth podile htta aitifacsetl heorydng gninod:b a ehyrgdon bodnu to a logsyrnt egeitlonvtcaree uolemcle liek efliroun iwll area”p“p oerm itvoeips and, u,hst ed-hrydnoonbg eomr lnstgyor htwi a nyreba ognyxe mrpedo(ca iwht a ngehyrod cncneodte ot ob,nacr fro epal.e)xm
ureFthr andiegr:
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 tgmhi be nkgonhireivt ti t,ub H onbd ftimoaron fo aas' kasme the sencodyra ertsucurt of eht rintoep oaelncgl( in stih )aces. ehT yGl to aAl tubisitunots sdeo rslute ni sels H dobn oafi,mtonr utb of nididuvali 'asa ont wenbtee lngaecol eesomullc (tath itmhg eb eorm for uyreaqartn tcestu)rur
rraPiym ctsurretu = oanmi idac nsaurdq yecnceeoSe urrtucste = etrurtusc mdreof hwti a neligs noima daci sueeqecn eb(at eptlaed ,etesh phala ,lxeih eyr aic)eTttr ecrtutrus = leumitpl ernycdaos sttucrersu rtianitngce gothrtee pimulte(l abte tadeelp estshe skadcet on pot fo ehac hoetr, eerya trrc)tQuan sueucrrtt = tpniore ettcrusur mfdero rfom ilfndog of lla tearyitr rrteustscu ot eakm ginidbn setsi, .tce
Secin the elinana aws utp in plaec fo eth ilc,ynGe het yirparm tucurrtse swa ebuanl to mfor an aahlp hliex nices hpala xleih urstsceurt ened a tclrpiuraa qeunesce y(gl - -x )y in reord to fmro eyndrohg bonsd ot kepe hte lehix s.etbla
htwa si nglolace ? a aecyrosdn opeirtn .esurtrctu
wenh oyu mvreoe ,ylegicn eht smto tubdnaan aoimn diac , omfr het scrreurop elolumec lwli uyo teg a prrepo oarcydnes ututcrsre ? NO
yGl is p,ralo lAnniae si nropaonl nad hy.rbdchooip ssniMsee ensvonctaoreinv nttimuoa. hseTe AsA ahve eftfedrni hecimlca rrppteiose hwihc leda to upedsrdti penitor ngfliod eds(raynco .sert)utcur liarSim to lGu - laV sinuitsbtotu in Seilkc ellC Daes.sie
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$279$49I nhkit it ahs itosmehgn to od tihw cnyglei deu( to tis mllas eisz ti nca itf ni nmay aplesc rwehe ohetr ioanm sdcia acn nto nad neceh ti oisdperv lcarsu“rutt emso”ntsaccp to eth o,nlgalce .ie. utp a kkin ni the alhap i)xle.h If ygcneli is amlpesdci yb snmigoeht le,es I tndo’ khnit r-cgaploolne nac mrfo sti otrrcce edyocarsn rutecsr.tu
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