I de,ifrgu enyl-Xig-Yc si hieacllytcn ricdnedeso a “amryrpi nioam caid estrucutr fo a nepio”rt nicse teh nendfioiti of a ayiPrmr uscuettrr fo a netopir is “a rnilea ncaih fo inamo dasi.”c If uoy mses whti eht mryraiP eurrtcsu,t as ni teh qseituno setm, ouy nnctao rofm the edrSaycon ucetrtrsu of teh io,nrtep iwhhc is dneterdmei by the ddnhgn-nooybireg whhci orcscu tebeewn the idtpeep knbaeocb, idpedntnene of eht R osp.ugr I phoe thsi made e.snse
orFm deiapwkii: dacSe“noyr ucetrstur is fralyoml efiddne yb eht atpnret of nryodhge obdsn beewnte eth maoni ynoehdrg and oryxbcal ogxyen atsom in teh ietpdep bocbeakn.” esamih(sp em)ni
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.
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ihchw esman tath OI ash a giyclen tiubtitnssou dan erofehtr sti aluneb ot rmof a aoensydcr urc.sruutte
euD to scgnile'y aslml iesz, ti ecatesr k"n"ksi ni het aomin cadi qes.ceuen eesTh kiskn are ededen to torylrecc ofmr eht adercnsyo sucrteurt.
Other rs:senwa
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Rcella atth ieaec-llahshp dna eaesshtbte- aer sxleeamp of rdnoeacys rettrussu.c hisT anc be uoghtht fo a tomnafsniiaet fo het phlaa e.xilh
theNrAo awy ot get at ti si avi laiitio:mnne
.A odyrghne bogidnn ndowtul lelary gnahce ecnis eeinhtr nlaeian onr ylcigne are aB ol.pr lyG gt&; laA ntlsohud' cngaeh hwo pionerl is foemdiid I( mean ti L,ODUC if ereht was a ticsre ciehadnnr ro ehnotigms, ubt ton a eartg D).nrasew ngtihno ot eicdinat ahtt eoglnalc dntgoeaierd si rlatdee in essropne ot na AA suoi.itusbttn os,Al in teh otextcn fo OI whh(ic si eth ietspgernn ta,omlci)np we adayerl ownk hatt the molpebr d'otesn heva itgnnhay ot od twhi dotdeanegir, oemr ihwt teh ncaghe in conue.trEus /itrftncu Hleyntso t'ndo ownk.
Hser’e eno way to oeesintomfeaicr--lps eacsde“erd ondeodbynh-rg f:rotao”nmi ’mI ton a bgi fna of shit line fo n,egsraino but yhlnectliac aienlan as a side ugrpo sah remo egsydhn*ro ofr epnaltoti dgrhoeyn digobnn hant iglecyn:
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,So cia”tyl“hc,nel inaneal lwudo rmpeti ermo dn-georohbynd ron,itmafo hhiwc hitmg allwo uyo ot lmntaiiee ttah oi.ehcc
Taht dsi,a it semes oasltm iseibplsmo ot urel tuo ituwoht( eyvr nhceiclta eklewngdo ro meso pedivrdo lripeeanmetx dta)a ttah hte ihgltyls elarrg nieaanl edso not impiar egodrhyn ogdnbin tnwebee llonegac luocsmele iav itrsec tisap(al) einrfte.reecn In rimslpe trems, nices ienlnaa si rgr,ela you lwudo ihnkt htta it tmsu oohewms erieretfn hiwt het dogonrhynend-ibg taht srcouc iwht teh weplt-dyi nlyeigc.
---
lytrS*cti enkgip,as its’ tno het rbmune fo gnroyshed but oals teh thgernst fo eth podiel that leiatfcasti hyrgoden nib:ndog a hndrygoe dbuon to a gytorlsn geeaenttivocelr lclumoee ielk uroefiln llwi p”erp“aa meor tpiiveso ,dna ,hust hbeyo-ddonnrg rmoe rtylngso hiwt a ayrebn nexoyg epcmodr(a hitw a hrdyengo tccdnneeo ot rnc,oab rfo e)mxa.epl
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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 tgmih eb rigkihetnvno ti ut,b H obnd ioraomfnt fo a'sa msaek the oacdernsy ttesuurrc of eht tpinero (lgolcaen ni htis ae).cs ehT ylG to alA otnsbiusuitt oesd tsleur ni sesl H bdon fotnar,mio ubt of uiviaidldn aa's ton benewet eagllocn cmeoluels ta(th mithg eb eomr rfo uatenrqray tseurc)rtu
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eSnci teh alanien swa tup in cealp fo eth lncG,eiy the rpyaimr ureutrcst asw baueln to fmro an lhaap lhxei nseci lapha ilhex ssecutrrtu deen a laracptiur ceqensue g(yl - x- )y in eordr to mfor dgynheor donsb to epke eht exilh btea.sl
tawh is cegaolnl ? a sndoryeca eotinpr c.truurtes
hewn you eovrem glen,ciy het tmso ndntaaub oiman adci , mfro teh pcrrouser clemoelu lwli uoy teg a pprore yanrcsdeo rtcersutu ? ON
Gyl si ,palor nlnAaei si ornlnaop adn cprodhhy.iob esMsneis oneervvnstoncai u.inmtaot hTsee AAs haev rdetfinfe cmilchea roerpitesp iwchh aled ot ruedisdpt oitrnpe fniodgl sacenod(yr t)recuurts. Srliami to luG - alV ubsitsuotint in Secilk Cell aesD.esi
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$279$49I htkni it sah sgtmenhio to od hiwt niglecy eu(d to sti mlasl isez it acn tif ni yanm clesap erhwe toehr ionma dsiac nca otn dna nceeh it eposrvdi tsac“ultrur onetmcsacsp” ot het ogec,laln ie.. upt a kikn in eth halpa i.hx)le If gicenyl si siecplamd by mtngosehi l,see I dnt’o ihtkn -eplrgnoacol nac omrf tsi ocetrrc doercyans turrtsceu.
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