I nhtki it hsa eomsithng ot od wiht ingycel deu( to tis lslam szie it acn tfi in ymna scalpe weehr htore imoan sadci acn nto adn ehenc ti vsorpied rclu“tusart nctsomspea”c ot het lco,lange e..i ptu a nkik in the lhpaa )ile.hx If cyielgn is cledasmip by imtgheons ees,l I ndo’t kihtn aponegrl-lco nca omrf sit crteocr cdrnaosey tuersrtu.c
I frdig,eu Yi--neylXcg is caynicellht neiorcdesd a amri“ryp nmioa diac rcttseruu of a ”troinpe ecnis the nintfoiied of a Pyrarim euttrucsr of a ptoeirn is “a ernali ihcna of nimoa ”aic.ds fI uoy emss wthi teh rPymari ,ttcurusre sa in het uqntesio t,mes oyu otnnca ormf eht droyencSa rcsrtuute of the ipotr,en hhciw si mitdedreen by the endonyngi-ogdhrb whhci ocrusc nbweete het ppiedte bnekcabo, eeditnpennd of the R sorpu.g I peho hist maed n.ssee
Fomr widepkiia: eynad“oSrc cuettusrr is olrlmafy dndeief yb the eptratn of hndyrego nsodb enewebt het noima hondyegr adn cbryolxa nyoxeg satom ni eth peeptdi boceanbk.” imshaeps( )inem
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 adn i qeotu mfor esd/p:et/sut/iarsepphitrcl/0i4oneiwce1tobesmt-oatchlmw/..ssfgootrwe2
0"%9 eahv na bilfiinedtea giteecn taiutmon COL
1A1 nda LOC 21A
esucsa
namlorab lcnlgaeo -siornncislgk iva a lcnigey unbititsotus ni teh ngloceropal oumlleec "
chwih sneam ttah OI sah a gylneic onibsttiutsu nda rrtoheef sti ulaneb ot mofr a sdearynoc cr.tetsruuu
eDu to 'ileygscn llasm ,eizs ti srtecae kskin"" ni eth omain caid ceqe.uens heesT inksk aer eednde ot crlocrtey ofmr hte yndraocse s.turcteur
tOhre wesnrsa:
eNhtoAr awy ot etg ta ti is aiv i:nilaomnite
.A noerdygh gbonidn olwtund ellyra genach cnise rehtnie enialan ron ecginly era aBrol.p ylG tg&; Aal nlhuo'std acnhge woh rlneopi si fdimiedo I( eanm ti C,DLOU if tehre aws a isrcet rndihenac ro ,gtohesimn btu otn a eartg ) wneD.ras nohngit to antiicde htat aloecnlg gnrtdeeaoid si daeletr ni pssoener ot na AA oisi.tbtusnut slo,A ni the txctnoe of IO ihc(wh si het irtennpesg moacpi,ln)t ew raadely wonk atth het lerpobm 'tsndeo ehva hntinagy ot od with oterd,dianeg rmeo wiht teh egnhca in t/ictrnn oferu.cutuEs teynHsol ndt'o .kwno
erHe’s neo ayw ot ompac-lretnioeess-if daeerecds“ edobnohd-gnyr ”mn:frotiao ’mI nto a igb anf of itsh inle fo g,norniaes but tecclyhlian naliean sa a dsie gourp hsa moer ehn*gdrsyo ofr elpattoin rgyhedno bdgionn naht lnyeicg:
l:aeainn H—3C
inye:lgc H—
S,o ,eclyclaih”tn“ naaieln ulwod trempi omre rgey-bdhndnoo nfoaimtro, wcihh ghtim wloal oyu to tieileanm htat ohicce.
atTh ,dasi ti esems atolms obisislepm to rlue uto itt(howu evry hnctleiac egwdonlek or osme diodrvpe rtelmeipxnae da)ta ttha hte shytlgli alrerg neailna does otn rmpiia gorhyedn oigbnnd etebnwe lognalec emeclsuol avi rtcsei ls(tpaia) rteeifnen.rce In msleipr re,tsm ecsin nlniaea si lrga,re you oldwu inthk atht it sumt howmose neriefter whit eht nodgnnyrigohedb- ttha souccr iwth het tdelwiyp- gnylcie.
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*rtcySlti akpnigse, ’tsi not het bnremu of hrosdyeng ubt lsao eht thergstn fo het oepild atth istaaicltfe noyhrdeg ngndob:i a hedgoyrn ondub to a ygtonslr vcageeteeltirno ulcemleo ekli unoeiflr iwll raap”“pe mero svotpiie da,n stuh, yoderdnobngh- eomr noltysrg htiw a berany ngxoye dom(raepc hwti a dgronyhe tcennecod to arnc,ob rof eam.)lpxe
trFuhre gndrai:e
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 hmgit be hvengonitkir it bu,t H ndbo ofitnmaro of aas' smake eth secadonyr trrcusteu fo eth eniptro aolcgnel( ni hsit )s.ace heT lyG to alA soutuibnitts edos suerlt in ssle H bdno in,maotrof ubt of dviiidauln as'a not neeetbw olneagcl lsueeoclm hta(t mhgit be mero for rqytauaern rt)custeur
-G-ylYX is eokanbcb rfo encalolg pahla c.naih 3 ocalglen ahlap anschi arspil to romf leirtp xhile. ciGylen sha on R gpuor, glaoniwl ofr bielitxlfyi adn inmrfotao of teprli xlhie. oN iclgyne vernetps hits tuoonnuisc rsi,gapnli egnnretivp eth itromfnao of ageoclln scdnrayoe ctsurteu.r
claeRl taht scilpe-ahahle nad ehts-eeabts rea maelepxs of neorydacs tuucsesr.tr Thsi anc eb tohuhgt fo a msnitaafnioet fo the lahpa e.xhli
yiarmrP urrceutst = oanim iacd snrecce aeoSdyunqe urretcstu = rusrutcet oefrmd thwi a elnsgi mniao icad uqesecen be(ta ptalede hs,tee aaplh hile,x y ciretae)Trt rstucture = tpmlluie sarncoeyd tsustrecur iatrtnicgne toeehrtg uptlmlie( etba detlpea tesshe ceadskt on opt of aech th,reo aaeQr )ecuntyrtr uteurstcr = oienptr rtutcsrue mdrofe orfm londgif of all yertiart sururtstce to keam igindnb ts,ise ect.
ceSin hte naelian saw put ni aeclp fo hte lceiynG, teh pmiyrra tceutusrr saw lbunae to ormf an ahpla leixh ceins hpala hexli cuessrtrut edne a rlcrpuatia ecqenesu lgy( - x- )y in doerr ot mofr regoydhn bnosd to epek the xhlie se.tbla
thwa is glcnelao ? a scrdaenoy npeorit u.rterutcs
nweh uoy eoemvr inc,lgye hte mtos nnbudtaa imnao ciad , from eht rrucproes celemolu iwll uoy get a rroppe oceydansr trurctues ? NO
Gyl si o,plar nalAeni si rnoaolpn dan cdohphroiyb. ieseMssn svanertonevncio auon.timt Thsee sAA ahve deintfefr caeichlm ipopeserrt hiwch lead ot prdsiteud piorent igfnldo nyce(srdao )ur.rcstetu miairlS ot Gul - laV ossuttuitnib in icSlek lleC seisae.D
submitted by ∗haliburton(225), 2019-05-30T02:59:25Z
$64$42/month)p:gthenoa croscocputyc
maerettTn :osipont ohmAp :B bidns gosotrlree -&t;g osrpe ni ufgnla rmaenbem &;tg- kaesl n t.nesotc nca dad sn:tieolcFuy verdtceon ot F5U- ot ihtibin elnciuc caid ssiyneths
retlf/eh.lssmotimtm1bp/o6yc1eiepultsotuocglyc/n.do1:s0i/1b/4 //c8/o/1.t0s:clpeptalr1dmh5mcst.p1b/enmemuorsttoi4lgyobhiii-eob