I dgrfe,iu iXyeg-l-Ync si lalnehccyit sdonceerdi a ampryi“r manoi icad ctertsuru of a e”rinpot ncesi eth fnneiitiod of a airPymr cutsruret fo a onerpti si a“ raenil icahn of amino d.”cisa If ouy msse twhi het Piymarr custuterr, as ni hte esutoqni ,mste uyo contna morf eht nSacdryeo rsurectut of teh pr,ointe whchi is rmetdieden yb het dngdogbny-oerinh hwihc csoruc ewteebn teh pidepte bocbnkae, detndnnpiee of eht R spruo.g I epoh itsh mdae nes.se
Form dkiwpeiia: arcSnode“y errsttcuu is lryamlfo eidfedn by the apretnt fo ordhygen sonbd ebentwe het ioman rhyoendg nda ycxbloar yxegon amsto ni eht edptipe obbkacne.” measi(phs mni)e
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 gusy dan i qteuo fmor f/rs0pa:sreletei/os/4et.dtmp/centchgaer1siim/te.2osuibhottowsco-wlwp
90%" eavh an ibeileidnfat ctenieg imttaonu C
LO 1A1 nda OLC 2A1
ssuaec
nmaraobl llcgnoea nngcssr-koili via a geycnil nsbusuotttii ni hte algleoorncp oleulmce "
hihcw asnem taht OI hsa a gcneliy biuttsntsoui nad ehtrofre its nabelu ot romf a noaserydc erucut.rtsu
uDe ot gsy'cienl amsll s,iez it esactre k"n"iks in hte mioan iadc cn.squeee hseeT snikk rea ndedee ot rtrcloeyc rfom eht nseydcaro .usrtctreu
hrteO sersn:aw
Yly--XG is naebckbo rfo elnlogca lhapa can.ih 3 ncgollae alahp nshaic rilspa ot form lrietp .hxile lGneyci has on R ,opgru aloliwng ofr lyxitbfiiel dna oairmontf fo ilpter li.exh No iyelgnc ntevpser htsi ontnuoicsu aigpr,snli eneipgrntv eth amnofitor of lelcoagn soceandry uutres.crt
eclRla thta elhp-iaclseha dan stee-estbah ear lexspaem fo dcnreyosa rsrsctt.uue ihTs cna be gtouhth of a antnaitfoeism of eht paalh .elihx
ANtoher ayw to egt at it si via tneinlioaim:
A. odgenhyr gidonnb dlotunw yraell neacgh nices eihtrne inalean orn ceiygln rea opa.lr B Gly &g;t lAa 'dolhusnt ncaheg woh nepiorl is eoimddif (I anme it ,LUDOC if rtehe wsa a restci ncdinreha or sg,htmeion tub nto a etgra n)sa e.wDr ghtnnio to daieictn ttha gancello enragdidtoe is rdtelea ni sonperes to na AA uuns.ostbttii osA,l ni eth ocexttn of OI hichw( is the epnniergst pa,oimnt)cl we aydrale knwo that the oelpbrm tosen'd hvea nniaghyt ot do itwh dr,iagonetde rmeo ihwt hte hacneg ni c/no.ntEsrc ufeiuurtt esolynHt tdn'o wkno.
Hre’es neo wya to mpoise-rect-aloienfs e“esarecdd eyoogn-nbdrhd ”a:mtifonro Im’ ont a big fna fo sthi ieln fo na,rnisoeg but yhcnalitecl ailnnea as a ides pgruo hsa remo nrsdo*ghey rfo altpionet nohgryde bndingo hnat ygcnlie:
iaanlne: C—3H
cnlg:yie —H
oS, y”ethinclc,l“a aelinna dulow ermitp oemr grhbdooeynd-n niftoom,ar hicwh tmigh oawll uyo to neemliita atht ce.icoh
athT sid,a it smees taloms imlssiebop ot ulre tou uo(iwtht vrey aehtnclci dwoekngle or soem pddervoi rpxemtneliae )atda that the hiygllst elrgra ennaial odes nto mpiiar ndhoeygr ngiodbn etwenbe loclneag oumelselc iva ertisc s)al(tiap e.icenrenretf nI smeplri mstr,e since liaenna is alegr,r oyu owlud ntkhi tath ti smut hoomsew neirrfete with teh nnyndbeghi-rdogo ttha orcucs wiht het etwypidl- neylicg.
---
rttSliyc* sknpige,a ’its ton hte ebrmnu of yehogdrsn but laso the hetgsntr fo eht ledoip ttha csfaaittlie oyhdreng ibon:dgn a ngeyhdro dobnu ot a oyrlngst noeeilrtvecateg lemcleou leki iofuernl wlil rap”epa“ omer itpovies adn, u,hts nydgoored-bhn rmoe tlysnorg with a ybrean oygxen moad(cper whit a nodyhegr ctdcneeon ot boa,crn rfo xelep)am.
rtFeruh :ngreiad
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 mtghi eb iitovknrnhge ti u,tb H bodn oamrifnto of s'aa eaksm eth raeycdson trcutruse of eth tnoipre ac(gelonl ni itsh .cs)ae eTh lGy to alA intststiuoub odse utsrle ni esls H bnod iafomntr,o but fo idvanliidu aa's ont nwbeeet eglonacl leecsuoml (hatt timgh be eomr rfo ayatnerqru r)uetctrsu
rmyiaPr trueuscrt = niamo aicd Seyeouencnerasc qd etusrtucr = ttrsucrue frdmeo ihtw a sgeiln maion daci ceqseeun eatb( ptldaee ,sheet haalp ehlxi, tceyarTti) re uerutsrtc = liltmuep dyeacorsn uttercussr inttirecang tgterheo uliepmt(l aetb aetledp tsehes tdksace on pto of haec eoth,r eruteQr ctra)yna truutserc = tropein truuctres ferdmo ofrm fldonig of lal aryreitt ersscurtut to aemk gdnibin s,etsi e.ct
cSein eht eninaal was tup ni eplca of eth Ge,cyiln the armpiyr cetusurtr wsa enbula to form na pahal xihel escni plaah hxlei ctetsrsruu edne a ptiualrarc equcnese gly( - -x y) ni drreo to rfom hryodgne nbsdo ot ekep eht ilxeh a.lsebt
awth si lgnlcoea ? a sdcnraoey ptioern utrrt.escu
newh you vromee clgn,iey the otms danunbat moain idca , frmo the oesrrucpr emulocle liwl uyo etg a peorrp nardcoyse retrtsuuc ? NO
Gly si ,oaplr leAainn si ralnoopn dna yr.hocdopibh sMeesisn ronnntievecvsao natou.mit hTsee AsA haev irdfentfe acemlihc rtpieesrpo cwhhi eald ot seipdrdtu rienpto fdnigol onedyca(sr .utrut)ecrs irliaSm ot lGu - aVl tbstionutisu in Seilck Clel .sseeaDi
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$279$49I hinkt ti hsa ohegntmsi ot do ihwt gcleniy (due to ist amsll sezi it can fit ni nyam claeps whree tohre omnai ascdi anc tno and cehne ti eoprdvis “tltuucrars maotsnsc”cpe ot teh gcnoelal, ..ei put a nikk ni eth lpaah .)xheli fI cnieylg si idecalmsp by msenthgoi se,el I dton’ nhtik lonageo-lpcr nac rmof ist ctrcore oysadcnre creuu.tstr
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