I gfiue,dr gyi-neXcl-Y is tyilnlhceca odecnerdis a pi“ymarr onami ciad trteusrcu fo a i”prteon esinc hte eftnodiini of a mPaiyrr uretutcrs fo a peinrot si a“ anilre anhci fo omian ”.dacis fI uyo essm iwth the arimPry r,stucetur sa ni hte eiuotnqs tm,se uoy canton omfr the orcSandey utrrectus of eth ntrpieo, wchhi si rtidneeemd by eht eognhdrng-ndboiy ihhcw usccro ewnetbe eth tideepp bacebkno, ndepeninted fo the R usrpgo. I pohe hsti aemd ee.ssn
oFmr ipikwdiea: droyanec“S cttrusuer is mfrlyalo inefded by eht antpter fo gdorhney sonbd wtbeene the amion rdygheno dna rbaclyxo ngeoxy stmao in eth edppeti nckbobae.” emishas(p )ienm
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 yusg dan i tueoq frmo ir1w/eifsph4s:eeocesp0lowmtontacs.-eshr/ti./co/aesg/utwl2pmoritbtdte
9"%0 aevh na bdainietefil ceetnig monttaiu CL
O A11 and LCO 2A1
sauc
se bmlnaoar llcgaoen snisgrikcnl-o aiv a nyiglec ntbtiuusisto ni eht ooarnlcegpl leoelmuc "
hwhic ensam atht OI sha a lgyeinc sittosuutbni dna hotrrefe ist bnleau to ormf a ordcanyse cu.ruetsurt
Deu ot ycgli'sen almls ,szie it cstaree nik"k"s in eht namoi daci uenee.sqc eTseh iknks era neddee to rcytcorel fmor the ardcoyens ecuttrus.r
reOth wses:arn
-X-YylG si ecbkanbo rof nalceogl alaph c.hnia 3 glcnaeol aahlp achins pilsar to rmfo eltpir xil.eh elGycni has on R ougp,r alilognw ofr yblilxtfeii nda mofnatoir of ptelri eh.ilx No gynelci tepevsnr this suoonuinct raspiigl,n egtprienvn teh miofnrtoa fo ncgoalel rsdaocnye rttr.eucsu
Rcleal hatt echsplhl-aiea dna easestthb-e ear xlspeeam of yndrcosae crtuu.sstre hTis can eb ughohtt of a iisanmeoftant fo het lphaa le.hix
hNotreA awy ot egt ta ti is avi :noaimetinil
A. erghdnoy ngdbnio oltwdun rllyae agchen scine iherten annelai onr neicylg ear aB.op lr lyG t&g; Aal 'tluhdnos naghec ohw poienrl si ideimdof (I neam it LCD,OU if ehert swa a etisrc nanercdhi or htomsiegn, tbu otn a retag we. r)Dsna ginhtno ot idneatic that lgceanol drenagedoti is adtreel in rseenosp ot an AA nttotiuubs.is Ao,sl in eht txonect of IO (hwhci si het tngesipenr p,cl)atimno we rlydeaa nokw ttah eth eolmrbp eotsnd' have atnighyn to od iwth tneo,daedgir mreo iwth the cgeahn in cicu.u eEutfr/otnrtsn elosynHt do'tn kno.w
’esrHe eon awy ot smreoticepe-s-onilfa “dcersdaee gbonrddhen-oy frt”oiaom:n ’mI ont a gib naf of sthi inle fo negrna,iso utb yeialtlchcn laennai sa a sdie rogpu sah rmeo ohsrg*dyne rfo olpientat edhyrong ongibnd thna engycil:
lanean:i HC3—
clyigne: —H
oS, nl,yahceic”“lt nlnaaei loudw pemtir erom gnodeh-bryond a,mofrtoni iwchh itgmh owall uoy ot aitmleien htat c.heioc
tTah ad,si ti meess tosmla pssibomile to leur tou ih(otwut eyrv nthiceacl deknewgol or eosm dovepdir leetnxrieamp )tdaa atht the yligsthl algrre lanneia seod nto irpima ondyeghr ngdbnoi ewtbene aenocllg osleelmcu iva itserc sata)i(lp n.neifcrertee nI lermpis serm,t esnic niaalne is earl,rg ouy duwol nhitk ttah ti mstu wshmeoo rinrfeeet twih hte yb-iognhnenogdrd atth uscocr hitw eth yplet-diw yieglnc.
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citrylSt* piaks,egn sti’ ton the ebnrum fo enyorhsdg tbu also teh tgernths of eht eodilp htta iataictefls grdeynho bdinno:g a eydnghor nbduo ot a yrsontlg egnartoveectiel lcemleuo leki oierulnf wlil rep”aap“ rome pvoietis and, s,tuh rogndhoy-dbne ermo yrnglost hiwt a nreaby gneoyx (dacrpeom wiht a rodyegnh cnctoeedn to raocbn, rof xpmela.e)
Furhetr g:driena
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 ihtmg be regvitinnohk it ,btu H obdn rftanioom of as'a amkes teh edyoacnsr eurttsrcu of teh ripteon a(glocnle in htis e.s)ca heT lyG ot Ala onuubsitstti odse strule in ssel H bnod t,anifromo ubt fo iidnvialud a'sa tno eewnteb onllgeac eueoclmls at(ht tighm eb more for rtquayeran ucrturet)s
imPayrr uttseurrc = onami icda oeSnccy dasrqeeune usrettruc = uurtrcets dfroem tiwh a ilsgne iaomn acid sqeuncee tb(ae pdlatee sehet, aaphl el,hxi ryTeitacre )t erttucrus = lleitpum adeocnsry etucrursst tnatinregic ehogttre lt(mepliu etab atdelpe shsete estdcak on pot fo echa hoe,tr ruaye rrettacQ)n utseurrtc = eoiprnt surtteucr ofdrme fomr noldgfi fo lal ityertra etrrctussu ot akme ngindbi e,itss tce.
Sneic het eanalni aws put ni aelcp fo hte lyeGci,n eht rpmriya rscuuttre saw ebauln ot mrfo an lhapa hxlie ecins alhpa ihlxe ctrsureuts ened a cilarutpar uqseeecn y(gl - x- )y in redor ot mrfo ogrydenh dbnso to eekp the heilx bat.lse
awth is ecangoll ? a ydasornce rnptioe csetutr.ur
wehn ouy vemoer ,ncglyei hte tsom bandtanu inoma iadc , mfor teh corrpeurs colemule lilw you gte a orpper rsadcoeny uttrercsu ? ON
ylG is por,al Aenailn si prnlonao dan rhopdcbo.hiy inssMsee tnsnvaeeoncivor .aotmuint ehseT AAs evah tfeefrnid hiecclma porrpeseit hhciw aled to depirsdtu roeiptn oifnldg (aoyredsnc c)settur.ur iSlarmi ot ulG - aVl tutniisobuts ni ilkSce lCle eeasisD.
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