I fgdue,ri inl-ycY-Xge si cyaltnhilec eonedriscd a y“mirapr aomni idca esrtrtucu fo a teinrpo” einsc the fdnioeinti fo a aymiPrr rruttuecs fo a teponri si “a aeirln icahn of omina aics.”d If ouy ssem whti hte Priraym surructe,t sa in the uosqneit ,mset yuo ancont fmro teh daSrecnoy esurctutr of eth prei,not wihch is eirmdedten by het yhgneonrdiog-ndb cwhhi srcuoc eeewtnb eht eitdppe knbcoeba, enenpidednt of hte R .pruogs I hepo tish daem snsee.
oFmr idipiekwa: “raSnedcoy srctuurte is rlfmoyla ieendfd by het pnttera of gdrhnyoe odbsn newtebe eht ionam gohdynre nad rybxclao yxoneg msato in the peeidpt knaboecb”. samphi(es mi)ne
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 sugy dan i toqeu orfm opt.s.rbsww1totc-c0ossiep/moealit4ie/hohie/:dne//wmte2trusgtlafcerps
%0"9 hvea na iebneailtfid eingcet mtutonia O
CL 1A1 dna OLC A12
acsues
bonaarml eaoglncl ninclirskogs- vai a glnyiec ointttisbsuu ni the orlnoclepga uelmleco "
hihcw enams atht IO ash a gncyiel tionbssttuiu dna eefrrtoh tis nlueab to fmor a oercnsyda .strertuucu
Due to nygecisl' lalms e,zis it stecrae "sikn"k in teh iaonm cida .seueecqn Teseh knski rea endede ot ltcyocrer rmof eth nosydreac us.rurttec
trOeh :erasnws
-GylY-X si oknbbeac rfo agcenllo lhapa a.ihnc 3 ecaonllg pahal hcnsai arpisl ot frmo teirlp hlixe. cGenyil ahs on R rgu,op nalligwo orf ftiyixlblie nda namtoirfo fo ptlier x.lhie oN nciylge erevpsnt siht ntnuiuocso rgn,piilsa pirgeentnv teh nomirfoat of allneogc reaydocns rrtcue.tus
aeclRl taht ec-phlashelai dan -shestebtae are alpxmees of sdonyeacr suerucstt.r Tshi acn eb htouhtg fo a siatoteiannfm fo teh paalh .hxlie
AhteorN yaw ot egt ta it si avi itlonmnei:ia
A. nogeyhrd nnoidgb wotndlu ellary hcagen cines theenri nnailea orn elgniyc are op.a lrB Gly &;gt lAa 'sdnotuhl gechna owh prileno is idfeodmi I( name it U,ODLC fi trhee wsa a rstcie icenahrnd ro tg,nhmeios tbu otn a egart wDr)n sea. ighnnto ot eitidacn taht gnlaocel eogriadtnde is areltde ni seoenrps to na AA btittons.siuu ol,As ni eth tonxtce fo OI whc(ih si the eestpngirn )i,molcptna ew alaredy nwko that eth bolmper n'odest ahev gitanhyn ot od ithw ndit,eaedgor mreo iwth hte hanecg ni ct/ntnsiu.uerrtfEc uo tyneosHl tnod' .ownk
r’esHe noe awy ot teonirc-im-olseafpse dseracee“d dnobhrneg-ody :onmoftri”a Im’ otn a big afn fo stih inle fo aneosring, tbu lecchailynt annaeli as a desi upgro ash orme eronhgysd* rof altenotpi eyodhrgn obgindn than ylncgie:
ea:aninl —3HC
ieclnyg: H—
o,S ll”“,ycihtcean anenali loudw ipterm reom enhnyogdrob-d fmrinoo,at cwihh mithg oalwl oyu to nimaletie hatt hcioce.
htaT ,dasi it seems mlasto imssploeib to ruel tou itu(hwto evyr cltaneich oldekengw ro meos vodeipdr ieertelmpaxn tad)a hatt teh ytlhslgi rrgeal niaeanl odse not marpii ndoyrghe dgonnbi neetebw aelolgcn clesuoelm iav etisrc isat(pl)a recetr.nenief nI rlpeism re,mst ceisn iaalnne is r,aerlg you would kthni tath ti sutm mseohwo rfteneier hwit het egrghyd-oninnobd hatt ccrous ithw het ildwtype- igynlec.
---
iltct*ySr p,ksngaei tis’ not hte enmbru fo orndgeyhs tub oasl eht tsgrehnt fo hte loiedp ahtt acesiaifltt dnegyhro nig:dbon a ogehndry oudnb to a nrtlsgyo oanereitctveegl leumolec leki eournlfi ilwl ”eap“apr emro sitipove ,adn tu,hs d-ynbhnrooegd rmoe olrngyts twih a yebran xyngeo pedrcamo( hwti a ehorgdny ntdecnoce ot ,ocbrna ofr elpe)max.
rrhtueF egdn:air
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 ghtmi eb ihornntevkgi it u,bt H dbno oatomifnr fo aas' emksa eht syrneacod tctrrueus fo the prntioe aegllco(n in stih ).csae heT lGy to Ala ouiitutsntsb sdoe sletur ni lsse H bodn amofrnto,i ubt of ulniavdidi 'aas nto nebtwee ocealgln eelucmlos ta(ht htmgi eb rmoe rfo auatqernry urtusrec)t
ryimaPr rtseutcur = nomia cdia rqSscueenac neeyod terrusuct = uturrtsec fmoerd wthi a gnleis omani acid qsneeuec tb(ae dlatepe et,she alpha le,ixh eerrTyt ic)at crueuttrs = mteulilp yrecandso rtrctuuess tcntrnieiga eetthogr mpli(eutl abet epetdla ehtess cdtasek on pot fo aehc ,hoetr Qa atrcy)enuterr cesrtrutu = prionet truecusrt ofdemr form lfdinog fo all iytrarte trcsueruts to kmae idnbgni tsi,es c.et
cSeni the naielna asw ptu in aplec fo het Geiyn,lc het ryampir cuttrrsue asw elbnau ot frmo na ahalp ilxeh escni lhaap xhile rusuresctt edne a aaicrrpltu csqneeeu lg(y - x- )y in orrde ot mrof derygohn odbns to ekep eht eihxl .ltesba
ahtw is oclaenlg ? a rynsdcaeo oretipn t.trurcues
ehnw uyo mevreo g,linyec eht msot atnubdan nomia icad , frmo eth rrcrsupoe culolmee illw uoy get a eporrp ascroyned uctsrteur ? NO
Gly is lra,op anelniA is onprlnoa adn choio.bhyprd eMssnies vionvrsonectane oumtint.a sTeeh AsA vaeh fneetirfd imhalcec reroesptip hihcw eadl ot urteddips rontepi idolfng naerodscy( setcru)tr.u maSiril to Glu - alV bnutosuitsti ni kcleSi llCe eD.iseas
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$279$49I hknti ti sha mteigosnh to od itwh ciyenlg (ued to sit slalm zies ti anc fit in yman ceapls rewhe oethr ainom csdai cna nto and eench it rsdviope rtc“rtalsuu csomesctnp”a ot hte lonagecl, e.i. ptu a kink in the apalh le.xhi) fI iglycne is mceipdlas yb gsmniohet ,slee I odtn’ ikhtn aonloergp-cl acn omfr sti ecrrcot rscneayod utruse.rct
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