I frdue,ig -XcneyYigl- si ctchliynela dicsrendeo a iprmayr“ ionam daci eutrutcrs fo a ritnoe”p nscie eth infinidoet fo a miayrrP trutceusr of a rioepnt is a“ rianle chnia fo nimoa a”sdci. If uoy esms htwi hte yPirram tuertucr,s as in the snitueoq esmt, uyo ntaonc rfmo teh nScrdyoae rruttceus fo eht i,pteonr hihcw is tdeeiemrnd yb het nrigdg-oonhedybn hwchi scrcou twbeene eht pepetid eanbbkco, ennindpedet fo the R so.rgpu I epho thsi adem .enses
orFm kdipwiaie: Soyn“edrca rresuuctt is olyrlamf edfendi yb teh tenartp fo oenhrdyg bnsod eeebtwn eht onmai dernygho nad ycarbxlo exnoyg asmot in the tdieepp bconeabk.” asiemsph( mnei)
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 gsyu dna i qtoue ofrm /artcmtc/osto/.wussoleepsm0/rtiepbsiagidt-t.sh2prnw4ieef:holweoc/t1e
%09" vahe an fteanedibiil ceetign imtuaton
LOC A11 dan OCL 12A
sasuec naorbaml celogaln iskrsonlig-cn iva a ncliyge btistuouisnt ni teh ceolanprglo oeemlulc "
cwhhi mnesa ttha IO sah a ilgeync suiobtstunti nad ertehfor ist balneu ot mofr a yncoardse utrtsuer.uc
Due ot elisn'gyc mllsa e,zis it rceeats snki"k" ni the amnoi acid snqce.uee esehT kinks ear eeeddn ot cctrrlyoe ofmr het yrcnesoda ueutrs.tcr
heOtr wsrea:ns
-Yy-lXG is ecbaknob for nlgeloca apalh an.chi 3 locnglae hapal cniahs rlpais to rfmo ltperi hxil.e cyGlnie ash on R u,opgr oglnliaw rfo teyiflibixl dan otinamofr fo eltipr .elhxi oN yiegcnl nesrptve shit tuncinouos ,aigirlspn ereignpvnt het maoiftrno of lconlgae carsdoeyn trurect.us
lecRal htta hhacl-eslaeip dan beateth-ess are lpxemsae of scoyarend trc.utssure This anc eb tthhoug of a itnosaamentif of het plhaa x.lhie
htNoreA ayw ot get ta ti si iva oiatinlmeni:
.A ohnygdre idognnb ontwdul ayrlel gehacn isenc neeirth nanaeil orn eyinlcg aer . raBpol Gyl ;&tg Aal otndluh's ncheag owh oeilrnp si idefmoid (I eman it UD,CLO fi heert swa a estric annhicedr ro t,hemisong btu ton a reatg nrD)w a.se ihnognt to acteiind htta caeolnlg terndaogdie si eeratld in onesresp ot an AA tbuisi.outtns A,ols in eht xcnotet of OI hhwc(i si eth sneipnegrt )anpto,ilmc ew rylaeda konw taht het polerbm netsdo' vhea ihngytan ot do iwth eitnardoeg,d oemr thiw hte nehagc in n.tt/eucsfo tirErucnu nsetHyol o'dnt wkno.
eresH’ one wya ot f-miplrcen-eesstaioo eedsd“earc yehdoob-dgnnr ”mt:nriofoa ’mI ont a big nfa of thsi ilen of sreoninga, tub hylcitalnce inealan sa a isde grupo ahs erom h*dgyrneos rfo ialtpteon ohrendgy ongdnib anth liencgy:
n:eialna C3—H
eliy:cng —H
S,o l“ec”,lcaytnih ieannal udolw pmteri omer yngdbdn-eorho foo,niratm hhicw ithmg lolaw oyu to nmilieate ttha echio.c
thTa s,dia it emses smaotl ieiosmbspl to eulr tuo uhowt(it very hnecalitc kldnwoege or oesm odevidrp nreatxlepmie aa)dt that teh tglylhsi rregla anealin osed tno irapmi nyrogehd oibgnnd ewtenbe logencal esmlucloe vai sricte (aia)stlp f.neteneecirr In limpres res,tm nsice nnaieal si r,agrle uoy would tnikh ttah ti usmt smhoowe rtfrienee hitw hte nghb-nndgrodyeio tath scuorc ihwt eht ty-epwldi yenlgic.
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t*Sriltcy pe,kasngi si’t otn eth unbmre of roghnysde btu aslo het nretgsht fo het ipoedl ttha fetsicaliat ygrhdoen giob:dnn a ghydoner donbu ot a tglrnoys velentaigteecro oeuecllm ekil nfliueor liwl ea”pp“ra more ievpsiot n,da usth, oohngb-drnedy emor yslgontr iwth a eabyrn yexngo mcde(opra hwit a ondrygeh eonnctdec ot rnbao,c rfo eax.l)emp
uehrrtF andgeir:
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 mhtig be rkhinniovteg it ub,t H bdno trfmoinoa fo 'asa ameks the sndyecrao tcetrrsuu fo teh oeirptn l(nglaeoc in hits c)s.ae Teh Gyl ot Ala ittbtuinusos eods erustl in sesl H bodn ,oroafmnti btu fo viialiddun 'saa nto betwnee egclnlao emselucol aht(t tihmg be moer rof nueaqraytr eursrt)cut
raryiPm strucerut = minoa daci oqsurecaceyd eSnne rcsrutteu = rutuserct ermdfo whit a isngle moian aicd suceqene eta(b pleetad ,thees plaah ie,lhx tr eie)ytcraT rucetutrs = ultilmep ycnrsaedo usetsrutcr incianrtteg orehgtte tpulie(ml aebt tpealed theses ekdtasc no opt fo ache rote,h certn) aQureyrat uttecrsru = nipetor cuttrsure fdmroe omrf nildogf of lal iretytra rusetsuctr ot kaem inbdngi tsi,es tec.
Sncei hte aiaenln wsa tpu in cplae fo eht yiGc,eln the irrpaym tuutrcres wsa anubel ot mfor na laaph ihlex iencs alpha eihxl srtecsutru dene a iractarplu ecuesqne gyl( - -x y) in orrde to frmo orgdyhen dsobn ot pkee hte hlxei ets.bal
wtah is leacongl ? a ysdcaneor itonerp sruttcrue.
nweh you evrmoe lieg,ycn eht tsmo dntaanub ianmo daic , mrof het prrresouc eomulcle wlli uoy egt a eorprp nsycraeod trrusutec ? NO
Gyl si al,orp eannAil si pnlornao nad i.yorhpbdoch nssiesMe eevcsanrotnionv ointtau.m eehTs AAs aevh rifeednft acielhmc ertesrpipo cwhih leda to deurisptd tpernoi gdlnoif rcaoned(ys re.tuu)crts rmSiial ot lGu - Val suntiuttbosi in ilkSce ellC .Desesai
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$279$49I ktihn ti sha itomgehsn ot od htiw yegcinl ud(e ot tsi allsm sezi it cna itf in nyma esapcl wrhee hetor iaonm acsdi anc nto and eenhc it viopesdr raulust“tcr acspnoctes”m to het oagcllne, ..ei ptu a knki in het ahapl .)eihlx If iyecnlg is dsimlcaep by songmtehi else, I otnd’ hiknt lgnepa-cloro acn mfro sit etocrrc ordaeyscn tucterrs.u
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