I ,gdifeur ien-clygYX- si tianlcycehl cdrnsedioe a ymrairp“ onmia cida ettruscur of a ieor”pnt iscen hte oifnitdnei fo a rmPiray uesucrtrt fo a ieoptrn si a“ aliren hcani of oamin a.ds”ci If uoy emss whit het yirarPm cr,rtsetuu as ni eht soutiqen tems, ouy ctnoan romf hte ndSeyaorc uructetsr of teh niteo,rp hwich si nrieeddmet by hte hedbnoiryodnggn- ihchw ocursc enewetb eht eeditpp baconkeb, ndtedeniepn of het R rguops. I hepo ihts maed senes.
omFr dpieaiwik: cna“oedSyr tsucertru si yalfrlom eddfnei yb eht teartnp of dhngroey dbson ebenewt eht nmiao norhegyd dna boxrlyac nyexgo soatm ni the epetipd bconbeka”. (easmipsh e)mni
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 yugs nda i eutoq from i.powepe4weeicfrhsooalauccot.eth/tri1dtm2n/mpe-ogs/ibrl:estsw/t/ts0s
09%" vahe na fbiedntlaiei etcengi atunmoit
COL 1A1 dna LCO A21
asc
use amnolbra olcenagl gnklrsisn-cio vai a yelngic tbstuunitsio ni het oelplogranc eluelomc "
hwich nmaes atth IO has a lcyeign itutsiubsont nda tehforer tsi lenaub ot omrf a oycdranes .urstucertu
Deu to ynsic'lge allsm i,zes ti asreect n"kis"k ni eth aoinm idac eceqs.enu seheT kksin rea eedned ot cleyrocrt romf the ysrcdoena .utctrersu
rthOe aw:nesrs
GXl--Yy si bakebocn ofr lcalnoeg aplah hni.ca 3 nalgeclo aalph hnsaci sparil to orfm tirpel xhi.el Gciynle sah on R rgo,pu liolwgan rfo bifeyitxlil dna ootimnafr of epiltr i.helx No iyegncl vntsrepe hits oosctniuun spirlgani, egniptvnre het amornifot fo elcnalog rocaedyns uruettsr.c
Reallc hatt eca-islphleha adn hstsee-tabe rae sxemelpa fo oysrdeacn rutcu.terss shTi nac eb thguoth of a enosattaimfni of eth pahal lx.ieh
roAhtNe wya to get ta it si iav :tniilaomien
.A yhndogre obdngin nowudlt yelrla nhaecg eisnc ehitrne liannae nro cyeingl are rB.lpoa lyG t;g& Aal 'tulhsdno cnaghe who noilrpe is omdfeidi I( anme it C,LUDO fi heter wsa a citers cinhdrnae or htemon,sig but ont a gater w e)Dn.ars gthnnoi ot intdieac that galcnloe dignerteado si latered ni seeorsnp to an AA sntttsiiuobu. ols,A in eth ntcetox of OI (whhci si the eritpgnnse )olip,natcm we leradya kwno thta eth eplomrb steodn' avhe nhgaityn to do hitw n,drdtiegoae rome tiwh the hgcnea in u/ernctEciroutfn us.t oyHetlsn t'dno .wkon
rHe’es eon ayw to scslotim-e-pnoeraife edrcaede“s oyoeghdnn-dbr ofoiam:nt”r mI’ nto a gib naf of isht enli of insrgan,oe btu lalicycehnt ilanean sa a seid upgor sah roem ndrgeo*ysh for oetnipatl rongdyhe ibndnog tanh neilcyg:
eilann:a —3CH
cgy:ilne H—
,oS lc”cnilhtea“y, nnileaa odlwu mepirt mreo gododnh-ynber ifa,toomnr ciwhh tmhig loawl ouy to ineaemitl ttah hice.co
ahtT ,asid ti esesm msaotl lpisbmesoi to reul tou wht(uoit revy ieacnthcl egneklwdo or omse diovdper nelteaxeiprm ata)d thta eth lhylgits rrgale nalanie sdeo ont rmipia dohgnery gdibnno nteeebw caellong uecolmles aiv terisc )itpala(s t.erceenfrein nI miselpr tmers, nesic nailnea is arerg,l uoy wldou knith ttha it mtsu mwooesh iftrenree whti hte odgerdgnnhibny-o taht croscu iwth eht etdiw-ply cyeinlg.
---
y*tStcril enpkiag,s is’t not teh rnembu of rhosdeyng tbu soal eht setrthgn fo het lpeido tath tsltiiafcae hgdenryo gdobnin: a eondgyrh dubon to a sntgryol cgelotteiraeven eloumlce ilek nfruileo lliw preaa“p” eorm etiiovsp dn,a ,suht ondyghor-nbde emor lnysrotg whti a ybearn enyxog e(cordmap ihwt a gdenryoh cntneoecd ot na,broc rof ampeelx.)
theurFr dien:arg
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 imtgh be okhgtvriinen ti t,bu H bdon otfniroam of 'aas mskae eht snedoyrac rrcutuest fo hte otpiren ealgol(cn in hits )ca.es ehT lyG ot laA otinsibuutts edso tseurl ni lsse H ndob r,ifntmoao btu fo dauivnilid sa'a ont eentebw olecalgn olelcsmeu ht(ta tihmg be rmeo rof rurantyaqe urtsreu)ct
Pimyrar crrttusue = ioman aicd csyaqdeurn oneScee seuttucrr = trucustre eorfmd thiw a nigels ianmo caid nqeecsue tba(e pteaedl te,she hpala hlexi, r )eaeitycrTt tuuecsrtr = letumlpi decyarosn rueruststc nincettirag ttreehog umetl(ilp tabe ltpaede stsehe sakdetc on pto fo chea orhet, r)crayetarnQuet cerutruts = ietporn ruuetrsct rmfdoe mfro fgldoni fo lal aeirtryt tssecuurrt to ekam biidgnn s,eist .cet
ieScn eht nlineaa saw tup in pelac of eth eicnG,yl the rpryami erutursct wsa uanebl to rofm na aplah hxile nceis lapah elihx ssttecurur edne a lrrutpciaa queneesc (lyg - x- )y ni rrode ot rfmo dnoyhgre dobsn ot kpee the xehli ae.tbsl
ahtw si cnoleagl ? a ronsedyca tpinreo stt.eurcru
nhew you oevemr gn,ciyle eht stmo dnnbtaau aonim cadi , mrfo eht oupsrcrer omlecule liwl ouy teg a reropp aoercydsn ercutstur ? NO
lyG is arlo,p lnieanA is onnlrpoa dna h.rphoocbidy enisseMs tronvsevcinaeon aoi.nutmt Teshe AAs have enifedtfr ccemlaih otsieerppr hciwh dlae to udpiretsd onitrep fgndlio s(erydacno rut.eust)cr rSlaimi ot uGl - aVl isbtoutistun in ceklSi Cell eas.seDi
submitted by ∗wasabilateral(47)
It can be re-accessed by making a purchase.
Purchase your membership here
$279$49I ihtnk ti has hgteomnsi ot do iwth gyniecl ude( ot tis llsma szie ti acn fit ni yanm lapsce ehrew teroh noaim aicds acn ont adn ecnhe it vsoidpre tsruarutlc“ epctcas”mnos to eth nalg,eclo ..ei tpu a nkik in hte alpah ixh.)le fI cneiygl is acdsiempl yb tinhemgos sle,e I o’ndt nhitk oclgroe-plna anc orfm sti rcctero scrydoaen rus.cteutr
$279$49