I ufd,geir lXeY-ngi-cy si ycctlneilha idreodesnc a rmp“irya moani diac tteucsrru of a ienop”tr senic teh fnteoniiid of a Pmrariy tuucretsr of a nrpotie si a“ lneiar nachi of maion cai.”sd fI ouy smes hitw the raiPmyr u,utrcsert sa ni eht suqeotni sem,t yuo oatcnn fmor the raconydSe trrutcesu fo het rpeion,t ihcwh is eertmnedid by eth onhddrg-ginenboy hwhci oscrcu etnebwe eht pdeptie ebkabnco, epinnetdedn of teh R rgpus.o I heop sthi mdae e.ssen
mroF aiiekpwid: ey“aronSdc sreutruct si yarmllof dfdieen yb eth tearntp of hndroeyg dnbso bewtene eht naoim ndehroyg nda blocyxar enyoxg staom ni the depeitp oneabkcb.” speh(asim e)nim
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 ygus nda i tqeou rmfo a/eortp/1t4tisew/sstrw2ohsecrtn:iumg-ts.d.ospe//icleem0wbhlceotfiaop
9%"0 evha na eatdilfieibn ieegctn uottnmia L
CO 11A dan LOC 12A
es
suac balornam eogcanll rkgslosicni-n via a yielgcn stitiuntuobs ni het pcorngalelo mloeeucl "
chwih esman atht IO has a lcgeyni siobsuuitntt adn refhoetr sit bealun ot from a rcynesdoa utscurrue.t
eDu ot 'ylsgncei mslla izse, it asterce kk""nsi in eht naimo icad esnu.eecq heeTs sinkk rea eeddne ot yltrcorce morf hte rndcoaeys .etuutcrrs
terOh :wesrnas
-XGy-lY si oencbbak for aonlegcl halpa cinah. 3 agecolnl hpala ahncis apilsr ot rfmo lipret .iexhl elnGicy ahs on R gopu,r anlgwloi rof leiyftilibx nad aitfonmor of tperli x.iehl No icynegl tserpevn hsit uninostouc s,airlpgni pinrtnvege the tfmoaorin of nlagelco edynascor ruresct.tu
ceallR that eahle-icaslph adn -satbtehsee ear maxselep of doascrney uur.stcrtse Tshi nac be toguthh of a otifnsantamie of eht hapal leihx.
NAoreth yaw ot egt at ti is vai t:ioennliiam
A. goydhenr obnindg uowtdln larley hngace iecns nehriet lnenaia ron ylceing ear Bp.o lra Gly &;gt lAa th'ndolus ahgcne how rnlepoi si ddmieofi I( mane it UCLOD, fi herte saw a tsceri rhnidecan or egoimst,hn tub tno a trega awn s.erD) ohnigtn ot ednaiict ttah ganclloe gtnaoeiddre si rdlteea ni snroepse ot an AA btsuisut.toin l,soA ni het nctxoet of IO hc(wih is eht ntenpirseg ,pmnia)ctlo ew ledyraa wonk tath hte reobpml ds'toen haev ahngntyi to od wiht te,rodgnaedi roem with teh ncehag in .tsuc neEtofrrunuc/ti lntHoesy 'odnt know.
e’esrH eon ayw to etooia-ief-essclnpmr esc“ededra nedgoyrbnh-od rfnomiao”t: mI’ ton a gbi fan of ihst lnie fo ng,naersoi btu etihnlyaccl nelniaa sa a esid ruogp ahs omre eygr*hdnos orf ttonlaepi ehrdgnoy gnodibn thna nylgcie:
inaa:nle CH3—
:eglcniy H—
S,o al“,ltcynic”he leniana udolw imtrpe oemr dhgbrnodon-ey iroato,fmn ichhw hmgit lolaw uyo to iliametne ttah ceic.ho
ahtT adsi, ti meses molats bsmlpieosi to erlu out ti(hotwu yerv centahicl oeednlwkg ro smeo ipordvde enxlmritpeea )aatd hatt teh hglylsit lerrga enlniaa does otn amipri yrendhgo dbnigno neeetwb lgaelonc umecelsol vai sctrei ai(pal)st reerc.ennifet nI mpriels tr,ems csine lainena is gl,rrea uoy olwud nthki that ti stum oomhsew reefnerti hwti het erdinbndo-ngogyh htat sroccu ihwt hte p-ydiltwe igelcny.
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i*ltStcry snak,ipge sti’ otn hte enbrmu of degrhynso btu oals hte gtsrtenh fo eth oliedp atth ielftaastci enorghyd dning:bo a hodrngey bnudo to a tlygosnr leoevcnattreeig elmcuoel ilek rilufeno lwli rappa”e“ mreo oitevips n,da uh,st don-egobryhnd mreo rtsylgon with a raeybn oneygx mepr(coda thiw a gdrhynoe ccneodten to ,rbcnao ofr eemlax)p.
Fturehr nrga:edi
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 mhtgi eb erohkvtngini it b,ut H nobd rmoftiaon fo saa' emska eht oaynrcsed ttersuucr fo hte penorti lgln(ocea in hist .ace)s Teh lyG to Aal onstbuttuiis eosd luerst in lses H dnbo tni,fooarm tub of ilaiinvudd saa' ont ebneewt cloelgan uselmocle ttha( mihgt eb eorm fro rryneuqtaa u)sutcertr
ryPmria uerursttc = anmoi cdai qocSeecaeusyn rned rsceruttu = utrrstceu medrof hitw a enslgi amoni icda seeeqcnu (baet tdeaelp etes,h alpah ,lhxei yt)arTerte ic ucretrstu = luetmilp yrndsaeoc tescuurrts tirtgenaicn rtegothe pemlutl(i aetb pdatele sshtee sdeatkc no tpo fo echa hoert, renQt)eauract yr uurtrects = ieonptr utretusrc dfmreo mrfo oinflgd of lla yriatert rssucuertt to mkae bdingin ,tssei etc.
cSnie hte anliaen asw ptu in aeplc of eth nGyl,eic hte amrirpy rtrucuset asw enblua to rofm an lapah leihx incse apalh xlieh stuestcrur ende a urtpacrial enecques (gly - -x )y in orerd ot omrf dneyhgro ndbso to keep eht hxlei esalb.t
hatw is aenclglo ? a aryceosnd erpniot reructus.t
nhew yuo ovmree cnge,lyi het omst ndatnbua anmio dcia , morf eth rpscruore lleoeucm lilw uyo tge a rpproe esodyancr uutetrscr ? NO
lGy si rl,apo enaAlni si napnrolo dna yb.cdhhopori sMiseesn roeencnvaotnivs o.natimut sheTe AsA avhe tniefferd ahciecml erioserptp hhwic aled ot tuedsdirp tpeonir gnifdol o(nycsraed teurctur).s irmSlai ot uGl - aVl btotstsiuniu in ckiSel Cell Deaiess.
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$279$49I khtin it ahs omeshigtn to od wtih liycgne eud( to ist lmsla siez it cna ift ni nyam aepcls ehwre herto oinam csdai nca tno nda nceeh it isevropd rstcaul“tru ncot”psaemcs ot het gan,lecol .e.i tup a nkik in the alhap helx.i) If ieyclng is sadimcelp by eishgntmo e,lse I n’tod hnkit loa-orpenglc can orfm tis cretocr cdyesanor re.csruttu
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