I uf,edgir -ynelci-XgY is cylhntleica ndiecrsdoe a yrmirpa“ onmia icda utucstrer of a po”teirn senic hte ieofnditni fo a miayPrr sutreutrc of a pireont is “a einrla hnica fo moani d”.saic If oyu esms thiw hte mirPrya rceutu,str sa ni hte oenqiust me,ts uyo cnonta orfm eht arnyedSoc usurctret of teh er,onipt whhci is teneerimdd yb het yierggdbnodnhn-o wihhc cuocsr nbteewe hte ipeepdt ocnbkeab, idtndnenpee fo teh R r.uopsg I eohp tsih aedm ee.ssn
omFr ipwdiiake: onScryde“a ucsttruer is lyrmoafl feindde by teh ateprtn fo rhgodnye bnsdo eeetbwn het aonim dyoernhg nda xblcraoy gyenox mtaso ni hte etppide ecbokanb.” psesiamh( emi)n
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 ugys dan i otequ rofm htis2o/.asclios/w//.hsfwtsbamt0r4eptew/nrom1egdectisirpetolucepoe-:t
"90% ahve an fanidbeetlii nitegec inumotta
OCL A11 and CLO A21
uasces oralmban geocnlal nlni-skorgics aiv a cgyelni inutibusttso in hte nolaleorpcg mleceluo "
hwchi emsna hatt OI hsa a ncgyeli tniistuobsut dan fhtreero tis belanu to mfor a daycsonre .terucutsur
euD ot ngsycli'e lmals ,szie ti rctaees "nk"ksi ni eth iaomn dica n.uqeesce seehT snikk aer dneeed ot rccoryetl rfmo eth erdosacny surcteurt.
Oehtr earsws:n
YXGly-- si cobabekn rfo olceagln laahp cainh. 3 lneagolc pahla cainsh lpiras ot ofmr pretli h.leix yinecGl hsa on R o,gpur iwnoallg orf tyibfleixil dna fotinomar fo prilet xehli. oN neclyig esnptvre itsh nuonusicto rsp,lingia virnngteep the oiftnamro fo aglncloe onyrcesda tt.usurrec
Rlelca hatt eelhlcs-hpaia dan behsttes-ae rea asmlexep fo yraosnecd ssrut.turec isTh nca eb hthugto fo a ionafintsmtea fo teh halap xl.hei
AherNto wya ot gte ta it is aiv oet:iiilmnan
A. oyehdrng bidongn ltonuwd lraley anhecg iecsn nhterie ienanal nro lecgyni era lr aop.B lGy ;t&g alA lnothsd'u aneghc ohw replnio si fdoiedmi I( aemn it ,DLOUC fi ereht aws a srietc nacnierhd or s,mhotgnei utb nto a taerg rse.aD)wn tnghino ot teicanid hatt aleogcln eniaddteorg si dealrte ni eorsneps to na AA u.tiotsunsbit ,Aslo in het xtnetco of IO cihwh( is eht tpnregnsie alcipmotn,) ew raedayl wokn atth the lmepbro dnt'oes avhe nyniatgh to do iwht en,detgiardo mroe ihwt the acnegh ni ettsoEurc/uufi.ntcrn nslyHtoe o'tnd on.wk
’erHes one wya to ioi-nocr-tpleeafsmse eadder“ecs bngdh-dernoyo o”:nomatrfi mI’ nto a bgi fna fo stih ieln of ie,snrango ubt htceycllnai eannila as a desi uopgr has meor ydgrh*onse for aneloitpt redohyng iobgnnd tnha ngelicy:
aniel:na C3—H
inycegl: H—
S,o l”ilytccn,“hae nelaani lwodu ipertm eorm g-noehdrbnydo ti,frmonoa whchi mhgit wlloa you to tmeniiela ahtt c.hoice
athT ,sdia it semes omslta sobpieslmi to leru uto hottu(iw eryv ehccitnla lndewkeog or oems edipodrv expalermneti a)atd atth the lsihygtl earlrg neinaal osed ton maipir onyrghde dbngino nweteeb lnlgoeac mloeuslec aiv rtcsie atli(asp) crfinenr.teee In resmipl rste,m inesc inalean is arr,gle ouy ulwdo ihtkn thta it utms oweshmo nreertife tiwh eht hgrngnnibo-oddey atth rscuoc whti eth -pyldewti iclenyg.
---
tlyrSi*tc ag,npkeis sit’ not hte muenbr of drehygosn ubt aslo eht tsrnghte fo the opldie ahtt sfitacaltie neghrdyo ndinbg:o a nyrgheod odnbu to a glnrtsyo gneeiolaevtrtce luoeemcl lkie nioreflu ilwl epaa“r”p rmeo itopvesi dn,a ,utsh ho-edgrynonbd remo nstorgly tihw a banery ngyoxe eaomd(cpr hiwt a ehyrdgon ndtncceoe ot caborn, ofr el)mpea.x
utherFr deagrin:
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 mithg be enrgivkihton it b,ut H obnd amfioonrt fo as'a amske teh cnraesdoy tcreuurts fo the prtenoi gocln(ale in isht cesa). ehT lyG ot laA tuibttuossni osed uretsl in ssel H nodb ioaf,rtnmo btu fo vaidlndiiu s'aa not tenweeb canegoll sceoemull a(tht hgtim be roem ofr tquaarrnye urtucr)tse
mryiPar csuteurtr = omnai acdi cnnrea dqeeocuesSy tsuerruct = cuturerts rfoedm ithw a sielgn iaonm cida nqceeues atbe( tledpea heset, plaha ixeh,l ey)tTairrte c trterucus = mpeltuli ryneocads sutrcsretu nieactigntr ehttrgoe ultlep(mi etba ledtepa tesseh ksdaect no opt fo ahec reh,ot etrura )ncytaQre ctrtusreu = onrepit recttruus fedorm ormf dgnoilf of lal ryttaier stueustrrc ot eakm idbnnig estsi, tce.
iSecn het ilnaena was tpu in pecla of eth ,iGeycln the rrimapy rcsrtetuu aws unblae ot orfm na lhpaa lxihe isnec hlaap hxeil strueurstc need a ctrulpraia eqseuecn ygl( - -x )y in rdeor to romf donygerh nobsd ot pkee eht ihlxe l.esabt
ahwt is caeollgn ? a sonarycde ntiproe ucrt.etsur
wehn uyo mevoer ciyne,gl het omts nnduabta ioanm cdai , form het recouprsr lleumeco lilw ouy gte a rprepo dyecornas uerrtctsu ? NO
ylG si o,parl Aeliann si oraonlnp nad drcyhbipoo.h esnisMse esivtnoaenvnorc uot.iatnm eesTh sAA vhea iedtrenff iclceahm rprpetoesi chwih ldae ot rdtspediu ptieron lodnfgi sdryc(eona ce)ttr.uusr Slrmaii ot Gul - laV uibttosniust ni clSeik Clle saDi.see
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