I eg,firud lXcyYi-ng-e si cliecyhntal edesdcorin a iap“rrmy iamon idac urcteustr fo a reotnp”i nices het ndiinteofi of a mrayirP scrteurtu fo a onrpiet is “a eianrl ichan of inmoa id”a.cs If uoy ssme ithw eht Paimryr t,ucutserr sa in eht ntieqous ,mste yuo aoctnn mfro eht dSacreyno crtutesru of teh teinro,p hhwic is edneirmetd by the i-gnogdnoyenbhrd hcwhi rocsuc wetnbee het ppdiete kbcenabo, dndeientpne fo eth R p.urosg I eohp sthi made n.eses
mroF iaiweipdk: Scaye“dron truerctsu si ymlfalro ednfied yb the reattpn of eodnghyr onbsd wbeetne eth amoni genyhord nda yrbalcxo neoyxg atmso in the pditeep oekbncab.” iaemps(hs ni)em
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 usgy adn i uoqte omfr dt/sgl/aehi:etomloithie2atwstse/rtfw.oceppsb-w0ecrcsots.n1rm/4/pouei
"0%9 heav an ibflineitade nitgeec natotium CL
O 11A adn OLC 21A
s
ucesa lboaanmr aclenglo iolksgnsnc-ri avi a ngclyei stuuinsbtoit ni the pcalrgoloen lluemoec "
chihw msane ahtt OI sah a ygnlcei ntsstiouutib dna rthefreo sti unelba to frmo a rcdeasony usucrtrut.e
Deu ot lscg'ieny lsaml z,eis it trascee "kiskn" ni hte mioan icad een.uqecs esThe sikkn era eddeen to yrcctoelr rmfo hte cyasndore us.eutrrtc
hertO seswarn:
--YlXGy si bbaenkoc fro eolgncla alpha cna.ih 3 nloclgae ahlap hicans silrap to omfr ptrile .xheli icnylGe sah no R oupr,g wlanogil for xlfibyiteil nad orifntoma fo erplti hiexl. oN cngeily enprstev isth nuitonsuco ari,pnglis irntegnevp het frmoitnoa of alcgeoln dynsoecra erts.crutu
laRcle ttha eiaclh-alhpse nda es-esahtebt ear lpsmeaxe fo nyescardo tussr.cuetr hTsi anc be goutthh fo a eatfioanitmsn of the phala exi.hl
oehtrNA wya ot egt at ti is iva timnoaeiln:i
.A nhdeyrgo iodgnbn lwnduot aylerl cehnga inces nierhet aeiannl nro yncelgi rea r. paloB yGl &;gt lAa thudnols' gchane owh linpeor si oediidmf (I nmae it L,OUCD if ethre was a itersc ncaeihdnr ro osim,ethng but nto a aetgr eD wa)n.rs gtnoinh to acdtinei ttah lgeaocln aedtnogidre si rtdaele in sopesnre ot na AA sbnsitututoi. sA,ol ni the cxnoett fo OI hcih(w si eht erniesgptn i)pnto,almc we dyaalre nwko ttha the mrlebpo odns'te eahv ytaghinn to od whit deaedtn,irgo eorm hwti eht ehagnc in r nurtuoeEtunitcc/sf. neHyoslt 'nodt kwon.
s’eHre eno ywa to siotr-lnmcp-sofaeiee “dreeasedc yboordendhn-g namfoi”t:or mI’ otn a ibg nfa fo htsi inle fo g,oirneasn ubt icanelltchy eilaann sa a seid uorpg sah omer nhdsg*eroy for totielanp nyohedrg ngdnbio than gilnyec:
aanni:le 3—HC
yilc:eng —H
So, clacyle,nt”“ih aelnian ludwo emirtp eorm rnbdegyon-hod ,rtofoniam hhciw itmhg wloal yuo ot ateliemni that o.ceihc
hTat ,asdi it seesm stmaol ebilsimspo to reul uto to(uthiw vyer atehclcin wkogdlene or osme opvdedri iltermenpxea )data htat het tlghlyis relgar ilnneaa odse ont iirpma hdoegynr gboidnn newteeb olenagcl oemuslcle via ictres ipal)ast( itcreernee.fn nI sirmple stre,m ciesn nanilea si lare,rg you wlduo hktin thta ti tsmu ehoowms etefrerin tiwh hte nrygnboohn-idedg that rscouc hitw teh eldit-pwy ilcngey.
---
clrti*Syt nspiga,ke it’s nto hte uermnb of hrngodeys tbu oals eht httngsre of teh epliod htta ifsatlteica gyrhendo nbiondg: a yegnrhod bdnou ot a rgsyotln tvenetagcloiere umleceol klie lirouefn llwi reaapp”“ roem iiosvpet ad,n tsh,u hyoern-obndgd mroe tgsonlyr twih a berayn oxygne (odacprem wiht a nhgoeyrd tecondenc ot bon,rca rfo xlepe.)am
errFuht eigdna:r
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 ghmti eb gvhrientikno it bu,t H dbno oofmatirn fo saa' saekm teh sdoeynrca rrstuutce of eth eotnrip age(nlcol in hits a)cse. heT Gyl ot lAa intutousbits dose surelt ni slse H dnob f,amtioron btu fo naduiivlid a'as tno etewben ngoalelc lloecumse h(tta tgimh eb meor rof qurrayante uruce)rtts
ryaPrmi eutrcrsut = oainm acdi uaceyd nnSesrqceoe usetructr = rcustruet mroedf wthi a esgiln onaim daic quesence abet( epeatld th,see lhapa eh,ilx Trteai re)yct rsetrutuc = lptlumie soayndrec ertutssrcu ttagncrenii gerthtoe ltpeimlu( aetb pdeelta eeshts tdcaeks no pot fo aehc tr,hoe terrcau taneQ)yr etuursctr = onpetri utrtcsrue odmefr form nigdolf fo all rarityte surcusertt to amek inindbg s,ites t.ce
eSicn teh nliaean aws tup in calpe fo teh ,iceynlG het ryaripm urtcseutr was albuen to orfm na plhaa xehil sinec laaph xlhei srttecrusu dnee a arpiltcaru unseeqec (lgy - x- )y ni order to mofr ngyrheod dbson to ekpe teh xhlei easlbt.
athw is lgnacloe ? a dnoysrcae itrnpeo u.tustcrre
hewn yuo ervome geyil,nc eth tmso dtaunanb anmoi dcai , morf hte ercrrupso lleouemc ilwl ouy tge a rrppoe yadrscone tctseruur ? ON
Gly is a,lrpo laneinA si nloaopnr dan ociohrpbhd.y isseMesn oaveovtnesirncn niomtaut. sTehe sAA vahe nrfefdite lcceihma ipetesrpor ihhwc aled ot dtuiderps irntpeo nilgfdo racodnesy( u)trcusr.et limriaS ot uGl - Vla isutntutisob in klSiec lleC sD.iseae
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$279$49I iknht ti has ohenitmsg to do hiwt lnceyig ude( to tsi lsmal iezs ti anc fti ni mnay plcsea weehr reoth naoim adsci anc ont dna hence ti drpvisoe trsrlt“cauu epcc”nomsats to eht ace,olgln .e.i tpu a nkik in hte aaphl e)ihx.l fI eiclnyg si leapsdimc by stgmoneih esle, I ’otdn nhtik pengoclolar- cna rfom sit ccoterr aosrdyenc .rerttsucu
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