I f,geirdu n-gi-yYlXce si eclchiltany snidrdeoce a “ymiprra iamno adic etrtcsruu of a nrtieo”p ecsni teh idenifiton fo a Pmariry turercuts fo a tepiron is a“ lrniae nhcia of oainm asic.”d fI oyu esms wtih teh iymrPra ,euurttcsr as ni eth sqeiunto emts, you otnnca orfm het ardoneySc sruurtect of hte e,iroptn hhwci si ermeiedndt yb eth d-gdbonionehgnyr iwhch ccrsuo weneetb hte eteipdp bkecaobn, nndeeeidpnt fo eth R su.gpor I pohe hsit maed ssne.e
Frmo kiaipiwed: acdnyore“S utusrrcet si olmfraly infdede yb teh tpnreat of yordgenh snobd ebenewt the nomia ndegrhyo dna arbocyxl xoneyg oatms ni het edeppti necbokab.” hisaps(me nemi)
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.
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9%0" eavh an idiiantbleef igtence ttmiaonu L
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us
caes abarlnmo coglealn ici-nsorgknls iva a icyegnl tosiuintstub in the pngellocoar eomcllue "
ichwh eamsn that IO sha a gencliy tbiuunitssto dan teeforhr tis bulean ot mfor a syadcnero tre.uustruc
eDu ot s'nyigecl lmsal iezs, ti ctaerse n"i"skk in the oianm caid ceneue.qs eTehs ksikn rea needed ot tycoecrlr morf eht dnyraesco ttcesur.ru
hOetr :ensraws
XGlY-y- is ecobankb orf clglneoa lapha .ainhc 3 cleaongl hlapa iasnhc sprali to romf ipltre hei.lx eyniclG sha on R ,urpgo wnoillag orf ellixbytifi dna iarfomtno of iplter h.lixe No lcyngie eresvtpn thsi iutuncosno n,lprgiais peingrtenv hte rioamnfot of eocgllna dysearocn tureurs.ct
alcelR atth l-hcshepelaia dna hsebte-atse are elxpaems fo yrdaceson s.cuutrsret Tihs can eb hhuogtt of a eitnastmifona fo eht hlapa hxle.i
hNrtoAe wya ot egt ta it is vai ltieinaoni:m
A. hdrgynoe nidngob odtwuln rallye geahcn niesc ntheire aaninle nor nygclei aer lBpr.ao Gly ;gt& lAa t'ndulohs anehgc ohw rpnolei si mdodiife (I nema it OLC,DU fi teehr wsa a tcseri enhrcnaid or m,gitonhse ubt nto a tgaer sD).ear nw gnnothi ot ciaetnid htat conelalg edgiatonder is letreda ni epeosnsr ot na AA tn.iuiuostsbt lsA,o ni teh ntoextc fo OI (hcwhi si het nepetgnisr cmtnal)p,io ew rdaaely owkn thta het prbomle nesotd' evha hinatyng to do wtih ndtagoeird,e roem wthi hte gnecah ni u cionttrctE/rsen.uuf oltsHeny 'dnto n.owk
reesH’ one awy to timaero-eopsclf-nesi eersdace“d ehdyodnbgro-n rtiaoonfm”: Im’ ont a bgi afn of iths lein fo gornnsa,ie btu thyaenclcil ennilaa sa a idse goupr sah eomr yeshgdr*on rfo ntitopela nhgordye nbonigd thna cligyen:
naal:nei —HC3
ygcienl: —H
,So hela“cctny,li” naaenil uwold terpim more drnoyg-dhoenb amtnrofoi, whchi tgihm ollaw uoy ot ieenialmt htta c.ecoih
taTh is,ad ti messe mstaol eliiobmpss to rule uot (hittouw evyr ciltnceha glkenweod or eosm evddirpo aepnxtielrem daat) that het illyshgt aglrre neliana odse nto rpiiam oenrygdh bgidnon eetnbew clnaoegl meoclselu iva etrcsi aisp)(lat nefeeertcri.n In seprmil mtres, csnei eainnla is gelrar, ouy owlud tiknh atht ti mtsu sehomwo ierreften wiht hte onehoggibd-nrydn htta ruscco ithw eht ipldywte- neigycl.
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*ySltcrti gkaeips,n s’ti otn eth uemnrb fo deonshgry btu loas hte ngrtthes of eth oepdil ttha astilftacie ndegryho di:gnnob a rdgneyoh donbu ot a sgnrloty geeantetecilrov oellmecu ikel lueofrin lilw pr“apa”e meor vtpiseio da,n htu,s doerbnyn-hdgo rmoe lnysgtro ihtw a yrbena goenxy pmoed(car hwit a hdeonryg etcncnoed ot ,aonbcr orf ep)lm.exa
ruhterF ea:dnirg
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 tmgih be vnnkhiriotge ti ,tub H ondb taoromfin of 'aas easmk eht raoecysnd teutrursc fo teh rpienot nlol(agec ni shti s)ca.e The ylG to aAl nttsubtosiui esdo esutlr in essl H nodb noita,rmfo tbu of iduvialndi sa'a nto wtnbeee eglnaocl eeoscumll a(tht ihgmt eb omer orf eqnrryauat rrttuues)c
miyParr usutrrect = nomai dica Scaenqruoen sedyec suterurct = utcrrseut ormfde htwi a gelisn inoma acdi cnsqeeue bae(t dlapete ,sheet alaph ,ihelx ttearTy)cr ie uscrtteru = etimpull nyocserad tcrseusrut ianenrigctt trgteoeh itlle(pmu eabt tedlpea sheets tsdcake on top fo each terh,o yracrnuaQ)e rtte usutrecrt = irtonpe sretcrutu mdfoer mrfo glofidn of lal ritreaty urturessct to akme igbnind sits,e tec.
Sniec eht lnaeain asw upt in acple of eth l,yncGie eht iyrrmpa sttcreuru wsa ulnaeb to ofmr an aphla elxih csien palah ihlex ertturussc deen a aprrautlic sqenuece lg(y - -x )y ni odrre to rmfo nogrdhye dbnos to ekpe het hliex lab.set
athw si gnolaelc ? a dcoanerys onpreit turt.scrue
henw oyu omever ng,cieyl teh msot nantbuad aoinm caid , fmor eht osrecprur oucellem wlil yuo etg a orpepr anreodscy etcrustru ? NO
yGl si alorp, aeAnlin si oopralnn dna ho.orbipyhcd eessnsiM ovrnvcsnteanoie uiat.motn sheeT AsA evha dfifeertn emailcch eortippser hiwhc aeld to stuidrdep roeinpt idnglof r(dcyonsae ett.)urcsru rlimaiS ot ulG - lVa buostsiutnti ni kieSlc lelC .Desasei
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