I ir,fegdu XieYyc-l-ng si cnaleylchit eidcneodsr a “rrpmayi nmaoi dcai urturscte fo a ”eprnoti ecsni eth onnfdietii fo a irrmaPy rtrecuuts of a rpieotn is a“ ilenar hcnai fo ainom i.dcsa” If yuo essm ihtw eth riarPym treucrut,s sa ni hte nesituqo tems, uyo nonact rmfo the Snoracedy urtetsurc fo het opite,rn ihcwh is ddeenemrti by the rnebindoyggo-hnd wihch ocrucs eeewtbn eht pedepit nbcbokae, pintddeenne fo hte R sg.ourp I peoh hsti dame e.ssen
omrF kadwieiip: eSoca“nrdy rrceuttus is lrlafmyo deifned yb the ttnearp of ehyogrdn bsond netbeew the omain hnegrdyo dan byxcalor exyong sotma in the ppdteei eoabnckb.” mais(hpes mien)
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 gusy nad i teoqu rmfo .awohoets/ce1-pibsc/te.r/:olossectus4tpap2oi0nfrdei/ghtmiesltwem/trw
%09" vahe na iiltfiebaedn inctgee tmuainto L
OC A11 adn LCO 12A
su
ceas nlrobmaa nlgeoalc oirlksni-gcns via a yigcnle tbtnsstouuii in eht agnoolceplr eloeulmc "
ihwch amsen ahtt IO has a clnygei ttnsbiuiusot nad efethrro its nluabe ot fomr a docanyers .cuutrruets
eDu to cyenslgi' laslm sezi, it certeas kks"in" in teh oianm diac .neqeseuc seehT ikskn aer dnedee ot ecotylcrr rmfo eht casenrdyo e.cururtst
terhO s:aesnrw
-lYX-Gy is obcnakbe ofr cealnogl alpah cnaih. 3 laelcnog laahp nahisc sipalr to morf eriltp lehi.x lGencyi ahs on R rgpuo, wagonill rfo feiibllxyit nad mriftnaoo fo terpli x.hlie oN giylenc pesrnetv tihs tsconuonui pn,girasil nerevtngip teh ronaoitfm fo acoegnll nosyreadc ctu.resutr
cllRea hatt -clleeiahashp and tabsts-heee aer elmpxase fo doancryes utrrsseuct. ishT can eb hgtuoht fo a oftnaniamiste of hte paalh helix.
oANhert awy to tge at ti is iva iaiinoentlm:
.A yhengrod dnngobi dltunwo leryla hacneg nscie enehitr aalnine nor gliycne aer rpoalB. yGl &;gt laA nsulthdo' gehnac how prenloi is mfidoide I( maen it U,COLD if reeth swa a seritc rndiehcna or mn,sheotgi btu nto a terag .e)D nsarw thningo to idiecatn hatt noellacg genteoddria si areltde in repssneo ot na AA tsutiob.nsuit lAso, ni eht nxteoct of OI hw(hic si hte pnisergnet alpc,m)toin ew eyalrda wokn htta eth loepbmr oe'tdsn avhe yhigannt ot od itwh dgtdrenao,ei orem hitw het ecghan in it.nnostueEfcutcr ur/ yHtoenls o'dnt wok.n
’esHre neo awy to nmaoseifepserotcli-- r“dcseedea eo-bnydrgdnoh aotr:i”mfno I’m ton a igb naf of tsih enli of enor,nsgia but nlyctaicelh ialnnea as a sdie gprou hsa eorm rndsoeygh* rfo paontltei hodgeyrn gbonndi naht ingleyc:
liaenn:a HC3—
ieyl:cng H—
So, “lca,ite”nlyhc inneaal owuld ptrime orme bnoeoh-rydgnd fatnri,oom iwhhc itgmh lwoal oyu to linaietme atht h.coeci
tahT ,dasi it sesme malsot spbsmlioie to erul uot oitwh(ut evyr lhaceintc wognleekd or mose diodvper naemteirplxe dt)aa atht the ltilsyhg lregar anainel oeds nto mpiari dyrehgon oibgdnn ewenbte ganlolce lmuceeols via scetri aip(tlas) eirrn.fnetcee nI lersmip ,sterm ciesn nalneia is re,rgal ouy doluw intkh thta ti tums sowmeoh ifternere iwht eht hniry-oggdedonbn hatt cusrco with eth wyti-depl icygnel.
---
crtlitS*y epksgina, it’s ton teh bruenm of yersdhong btu alos het sthegtnr of eht lioped atht eitsfiaalct derynhgo :bngodin a yrgehodn odubn to a rgynltso enitetracgelveo emoleclu leki enurlfoi llwi ”apapre“ eorm opsvitei ,adn shu,t georhb-ynddon emro ltrsoyng thiw a aneybr neyogx cp(oermad hwit a oheydnrg cncdetone ot ,banorc rfo lmex).pae
huerrtF dag:rnei
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 htmig be nokrvntehigi ti u,bt H dbno oaimfnrot fo 'aas mesak teh scrndyaeo trusrtuec of eht itpreon noaclleg( ni hsit c).eas eTh Gyl to Aal itsutuontbis dsoe eusrtl ni lsse H nodb roifntm,ao btu fo dvuiilidna 'saa ont newbtee oganllce culolmese hta(t tihgm eb roem ofr tyuarrqena utsetcurr)
armiryP eucrsrutt = maino adic cdceaeSnurnso qeey truscreut = trutersuc eromdf wiht a inlgse nmoai diac ueqesnce teb(a eepaltd steeh, aplha ilxe,h eryctT ti)era ectsrurtu = tllpmeiu yadercson trutcruses nianitrtecg ghrotete tule(limp ateb tdlapee esseht ktcdesa on top fo cahe ore,ht a)te yenartQurcr turscetur = riopten ruttrescu dmefor fmro dlingof of all teyrirta erutrsctsu ot kame inidnbg s,ties cte.
cneiS eth inalnae saw utp ni acple fo eht ncGy,eli eht rpayrmi uecsutrtr was nbuael to omfr na haalp xlhie sneic halpa hliex tutseusrcr eden a rpracltiau eenqecus gl(y - -x )y ni orerd ot rmof ygdehnor dobns ot epek eth elxih eabl.ts
twha is loecnlga ? a snyreocad inorpet utr.ruscet
newh oyu oeverm eycg,inl hte tmos tbanuand oimna dica , omrf teh ourprrsec uleolmce illw you teg a ppreor acdneryos urcttsure ? ON
lyG is l,pora eaAnlin si opanolrn dan pbhiy.cdoohr Mssensei ervsnnetocoinav matin.tuo Teshe AAs evha edrfefnti ciemaclh spetoripre ihwhc aled ot edpsutrid treopni igofdln erdonas(yc rcsuut.er)t iSamrli ot lGu - Vla iuusnttiobts in elSkci ellC aseeDsi.
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$279$49I nihtk it sah tmshoenig to do ithw lgncyei (deu ot tsi llams size ti can itf ni nyam lcpeas rheew hoetr imnao cisad nca not nad ehnec ti sovpider rt“ltsrcuau oaspcesmc”tn ot hte ,galcolen i.e. upt a nkik ni het aphal i.leh)x fI cylineg si miepdcsla by othgnsemi lse,e I n’odt tnhik -anoclpgelro anc mfro sti rccrteo nrydeocas teuurcst.r
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