I re,gidfu gXil-cenyY- is naciychltel renseicdod a ay“primr mnioa dica sttruucer fo a rtienp”o sinec teh iionneftid of a mPriyar ectrsutur fo a eiortnp si a“ aerinl cnahi fo inaom c”.said fI uoy mses hiwt eth yamPrri sertcu,rtu sa in eht sqiuonet mse,t oyu tcaonn morf eth eracoyndS reuuttsrc fo teh ,onetpir whhci is eeenitddmr yb hte nindenyorhg-obdg hwich souccr enbeewt het eedpitp nabkobce, ndpeeitdnen of teh R sgou.rp I phoe isth mdea sne.es
rFmo eiidpiwka: yaenSo“rcd cttueurrs si mrloflay dedeifn yb eth rtnptae fo hynoegrd nsbod beewent eth animo gyednhor nad cbrxoyal gxneoy mtsoa in eth dppeiet ocbbkean”. i(sspameh n)mie
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 ugsy nad i uqeto fmor s/oetse:c/4tpierc-c1hpww.adletna/.sw0rrostugits2/th/eisiopbtfeommelo
%9"0 ahev an lnfiiatdeeib neiectg umatotin L
CO 1A1 nad OLC A12
ucsesa
oaablnrm ogllance gkscnsiilron- vai a ygnilec ottutsibunis ni teh rlpaolgonce ceelomlu "
iwhhc amnes htta OI ahs a ycenilg itntsbtiuous and tfrreoeh ist aeblnu ot frmo a yandrcseo usrteut.rcu
uDe ot cselingy' lsalm ,szei ti aertcse inks"k" ni hte imona idac eu.neeqcs Teshe skikn rea ddneee to rryectlco fmor the csyaordne tce.urturs
thOer nwse:sra
--YGXly si ekabnboc orf lgenaolc haapl .achni 3 glclnaoe paalh shnaic slrpai to fmro rlpeit hielx. ilnecGy sah no R rop,ug oillnawg for fixybelliti and romtoinaf fo ptrlie xli.he oN ynlcgie nvpeestr hsit ouontucisn npi,alrisg pnreviengt hte aormtfoin of olcanegl dcrnayoes cttuu.rres
aeclRl htat hlhpai-ecelas nda s-athseetbe era pameslex fo dnaycoesr cutrsrut.se hTis anc eb tuthgho of a mtsafoeaiintn fo het alhpa el.hix
ArtNeho awy ot egt at it si avi :ieoiitnmnla
.A ndegoyhr gnodnbi wdtolnu arlely ngaehc ecsin henetir ianenla ron cyenlgi era rlo.pBa Gly ;gt& Ala hdoluns't ecgnha ohw onprlei si ieofiddm (I mane ti DOCLU, fi heert wsa a cistre erhiadnnc or mg,hiensot ubt nto a agert )e .rwDnas tognnhi to dceiatin thta eognacll droteadeing si arletde ni rnpeeoss to na AA usson.titubit os,Al ni teh cnxetot fo OI ich(wh is teh srpeetingn ipco,la)tmn ew rlyeada kwon atht teh emlpbor 'odetsn veah iayntnhg ot od iwth naod,getiedr rmoe wiht eht ehncag in rcrsuofn cEtt.n/eiutu oteyHlns 'nodt nk.wo
rees’H neo ywa ot ten-lsofaepiorsmec-i ser“cdadee deoby-rhgnnod io”:tafromn m’I ton a gbi fna of iths inle of r,ainonesg tub elhlacyicnt anenial as a edsi oprug ahs erom n*dgyrheso rfo pntloatie yherdgno ngbiond hnat ynleicg:
eani:nal C3H—
nceyil:g H—
oS, laccni,t“eh”yl leainan odlwu tmepri roem onyhd-rbodgne fntim,roao ihhcw tmigh oawll you ot eimnetlai hatt ochi.ec
ahTt ,idas it essme mtoals psileoibsm to rule otu i(wuohtt eyrv nhelcciat oenwdkegl or moes pdrioevd ntplexereaim t)daa htta eth lyihltgs geralr nanilae esod ton mrpaii ehdynorg ngbidon weenteb oecnallg selmcleuo aiv tecisr pa)ialst( eeifrennre.tc In srpmiel ,mters nisec nenaila is ae,rrlg yuo uwdol khitn htta it tmsu oswehmo ernirefet whti het n-oenydbigornhgd ttah ocsruc with eth el-wipytd ylcengi.
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Scrtity*l psgak,nie ’tis otn the bnermu of rgdynesoh tbu sloa eht enhgrstt fo the eipodl ttha laficttaeis hydonger ngd:obni a hogndery dnubo ot a sntoylrg ctraeeotlenevgi leolumec ikel liouenfr liwl ar“”ppea reom piotvise nda, ,usht hognoyrbn-ded remo stlygorn wiht a ynaebr gynexo m(ocdrape iwht a orgyhden coendntce ot nobc,ra ofr .)aempxel
Fturreh aeigndr:
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 hmtgi be thiknvgreoin ti bu,t H dobn otniomfra of aa's asemk teh ynsrcaedo trsuetruc fo het oprinte la(genolc in ihts e.cas) The lyG ot Aal tuinbiottsus dose srletu in ssel H ndbo otorianfm, btu of iaudldivin sa'a nto weenebt cogllnae meleocslu atth( hgimt be ermo rof etryaaqunr suru)tcetr
iPmarry trrecutsu = naoim daci qSecs euncyodnerae esrutcutr = tcurtseru odferm ihwt a egnlsi ianom aidc eunecqes (beta peleatd ,etehs pahla h,xile erTtt e)icyra scturuetr = meptllui ecrnysoda tcrrutseus icgnttaneri etorhegt mlletiu(p etab etaplde teessh dkctsae on pot of ahce tehr,o ratr)euertQacyn rtsruetcu = nripoet errustutc omefrd mrof gfdlnio fo lla trytaeir ctrseuusrt to eamk igbnind ,tsise te.c
Sicne teh niealan swa utp ni acepl of the ,ineylcG het rriapym rrtuctseu was leanub ot form an aaphl ihelx cneis phlaa xielh tstrruecus dnee a iclapatrur eseuqcne (gyl - x- )y ni redro to rfom oehynrdg nbsdo ot peke eht lxieh lea.stb
twha is enllcgao ? a oandyescr eitpnro utectrs.ur
enhw oyu eemrov nilcey,g eht mtos anuntdab namoi caid , rmof eht rcrerosup leeuocml iwll uyo get a rerppo dsyonacer ruscuetrt ? ON
lyG is ,rpola aneAiln is nnparool nda iocyprb.hhod nMissees intonsvvaroenec .untimaot sheeT sAA haev dnrfeetif hacelicm ppotrisere iwhhc ldae ot eddiurpts entriop oildfng (ydonaresc rrtcuestu). lrmiSia to uGl - laV oiunutbssitt ni Sickle Clel eseiaD.s
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$279$49I hnikt ti has hosemnitg ot od tihw nyiclge ued( to ist slmla izes ti acn fit in mnay epaslc ewhre rtohe maino ascdi can not dna hceen ti vpodrsie stuarcturl“ a”ectonmpssc ot hte lnlecg,oa .ie. utp a ikkn ni teh hpala ihexl.) fI egcinyl si pmicdlesa yb nhieomtgs lse,e I tnd’o kinht opalcogrl-ne acn fmro tis torcrec doeynarcs rtct.ureus
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