I i,edugfr lcXgeyn--iY is thanllyicec rseodiedcn a ipyam“rr nmoia dcia uetctrsur of a ”ioepnrt ensic teh infetoiind of a airrmyP tsrcutuer fo a tripnoe is a“ iealnr nicah fo nmoia a”dsci. If oyu ssme wtih teh Pmyiarr ,suuctrrte as in hte nuqsteoi m,tes uyo ncnota omrf teh Sncdoeayr ureuttsrc fo hte o,priten chihw si etmiernedd yb hte nhgy-nodiogerndb ihwhc srocuc ebwneet teh eetpdpi eoancbkb, pedneindnte of hte R .spogur I ophe siht daem se.nse
rFmo iiwdipake: y“dSnoarec rruusectt is ollymafr fdieedn yb the ntprtea fo ydgeorhn nbdos etbnewe hte nioma gnodhyer nad rcaybolx yngxoe saomt ni het tdeppei aekbocbn.” ps(msihea )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 syug dna i ouetq mfro iltlooig/s/pac2hnit4srttscmt/tesaepmct:see.pfhoew0erso.ibd/wu1o/e-wr
%9"0 vaeh an ieblefnitiad egectni oumnttai
COL A11 nad LOC 12A
acssue mornalba ncagolle iirlscokns-gn aiv a clgynei iobssiuttunt ni eth orlgaoplenc olulcmee "
ihhwc nsaem tath OI sha a iyegncl ttnsiosbituu nad hoerrtef ist nuealb ot omfr a nscaydero ur.reuutcst
eDu to 'gisceyln mlasl zeis, it tscaere k""kins in hte inaom iacd qen.ecseu seThe snkki rea needed to ccrtreloy morf teh oeasnycrd .utrruetsc
trhOe n:arwsse
-lX-yGY is beknocba for elgncola phala ch.nia 3 lcnaelgo lhapa inchas iarpls to mrof rptiel xei.lh Gcyniel sah on R p,ourg aiwlngol orf fbletyiixil nda fminaootr fo rtipel xh.lei No neycgil vtreensp hsti ontucnosiu rp,aisigln erevtngipn the fiomnaotr of gaecloln raecyonsd ursetr.tuc
elcRla atht l-eshhaeilpca adn abteeet-hss aer elpxamse of yrscnoeda css.rrttueu sihT can be hugtoth of a snaofmaittnei fo het alahp hlxie.
heAtoNr way to get ta ti is iav nilni:ioeamt
.A oehnydrg nibdgon tdulwno rllyea nhgeca censi tieernh alenian rno clgniey are pBl aor. Gly ;t&g Aal sdolt'hun gacenh who rnloipe is dieimdfo I( aenm it ULCDO, fi rtehe was a erctsi direchnan ro smitoehgn, ubt ton a tgear aD)rne w.s ghiotnn ot ncietida ttah nlgleoac dtedagieorn is laetdre in neseopsr ot an AA uiusntbt.iots osA,l in hte xttoenc fo IO hhi(cw si teh trnpeengis lom,nit)acp we rdlaaey wnko ttah hte opbrlem tdso'ne hvea nngahyti to do ihwt iadtrgnoe,de moer tihw eht cngeah in u/n .fctuutrorneictEs lysetHon n'tod .knwo
’eHser neo wya ot -nmcarl-soesefptiioe easder“edc -onoegyrhdnbd af”:trinoom ’mI nto a ibg naf of shit neil of ran,gesnoi but yhaitnclelc naalnei sa a ised opurg hsa omer deg*nyohrs fro tlotineap ryoehdgn ndgonib anth ncyleig:
in:eanla —CH3
ynicl:ge H—
,So l“in,tcehcy”la neaanli odulw premit emor ebnryndod-hog ofaitno,rm whchi ghtim loawl uoy ot elnimeita thta cieho.c
Tath sid,a it semes mtolsa oblsipmsie ot uler otu ui(twoth vrey nahictecl wgeokndle ro esom vrdioedp xreeltmpinea tda)a atht the llsytghi rgealr inaealn osde ont mpiria dhonregy ognibdn entwebe lcnegaol ocleemuls aiv cietsr tap(ai)sl rfceeee.nnitr In rilemsp ets,mr nsiec ialenan is ,lerrga you loudw nhkit thta ti sumt wsmehoo trnefiree ihtw eth ngiegnydnr-oobhd htat rcsocu ihtw eth ywpil-tde ngilcye.
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Sct*yltir ,gpaskien sti’ ont eth urenbm fo sogheyrdn tub oals eht sgtrtnhe fo eht edliop htat ietclaafits genodyrh onig:bnd a hdogenry odbun ot a lysogtnr eveltranioegcte llceuome ilke lirnufoe wlil eaappr”“ orem oetpisvi dna, ust,h dgnyoo-erbnhd erom ynsglotr twih a yabner oygexn pdcore(ma thwi a drhnoyge nntcceode ot ,orncab ofr ap)ee.mlx
hFterur anir:gde
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 igthm eb hnregiktvion ti u,tb H bdno nfmoraiot of aa's smkae eht syrnaoedc rtecrusut of hte ointper olnegla(c ni tshi sa.e)c The Gly to Ala uusbntsittoi dseo rleuts in lses H bnod mntafiroo, tub fo niividdlua a'sa ont neetbwe clgoanle sulolemec (htta mhgti eb oerm ofr rynteuraqa )reutrucst
iyPrmra srtucrute = maion aidc Sqdrcaeeeocnsneuy ucseuttrr = tesrucrut fmdoer htwi a nieslg miaon aidc eqeuecns at(be elpedat ,teseh plhaa e,hxli eeyar)tTr cit tcrutrseu = imtleulp oacyndrse rrusutcste rtnneitcgia hgoettre ilpmlute( eatb tdelpea sstehe tscdeka on pot of ehca eothr, tarr)anecyeu rQt scrtuetru = inptero cuutsretr mfdore omrf ndloigf fo lal rtearyti ttuurrssce to maek dinbnig siste, c.et
ceSni eht aalnein swa ptu ni lepca fo hte ,neGcliy het pairmry ruuserctt saw eluban ot mfor an alpah hlxei esnic aahlp hexil ctuurrsest nede a trcuiarlpa seqecnue g(yl - x- )y ni errdo to mrof drgyhoen bonsd ot ekpe the xleih .ltsbea
atwh is cnoglael ? a dcryaeons ernipto rutuctse.r
nwhe you eremov nei,lgyc the sotm nndatbau noima icda , ofmr eht epurcrsro eomlulec illw uoy teg a erropp dsoycenra eutsturrc ? ON
ylG si pr,loa ealnniA is aonnplor nad ychopbr.oihd iMseessn nvnetsvoenrioac t.oamiutn seeTh AsA vahe rnteideff ehcmlcia reippsroet whihc aled to dsupedrti nreotip lingofd (adyocnser .sur)teuctr irliSma ot luG - Val tniisottbuus in kcleSi lelC i.aseesD
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$279$49I tikhn ti ahs isohtmeng ot od wthi einclgy d(eu ot sti lmals szie ti anc ift ni many lcapse ehwer othre nmaoi acsdi can ont and neceh it isprdevo stltrcua“ur m”oencpstcsa ot het le,ngaolc e.i. tpu a ikkn ni hte hapla .xi)elh fI yeicgnl si sedmlacpi yb ohsgminte sel,e I ’dnto ntihk gaencor-ollp cna rmof tis teorrcc oyndecsar u.terstcur
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