I ufdrig,e il-gncXY-ey si ylhlintceac ddeoecrnsi a pia“myrr manio icad trercstuu of a irentop” nicse eht idniofinte fo a ymiParr cursuetrt of a teoinrp si a“ enrail ihcna of oiamn i”adcs. fI uoy sesm iwth het ayiPrrm crru,ettsu as ni the oqutiens et,ms uyo nantco rmfo the edoayScrn custuretr fo eht tiropen, hhciw is dedeiremtn by eht nbr-godiedgynhon hhcwi ocrcsu ewetebn eth eepdtip acnekobb, dietnpneedn fo het R pgrou.s I peoh ihts maed eenss.
Frmo aiewkdpii: nec“oydrSa utsrcuter si mlflrayo nfddiee yb the pnarett fo hrdogeny dnosb teebnew the iamno noheydrg nda yaoxbrlc gyenox asomt in teh pepietd ecknobba”. ihsae(pms iem)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 gsyu and i toueq ofmr -sw.i4ieeeetpt:fgre/srawoo/hawbstno/m//tomu1pr0ts2ei.lldcttissopcceh
"0%9 eahv na bdilaefeinit ctngeie otanmtui O
CL 1A1 and COL 21A
scues
a arolmbna aelogcnl lsckrn-gisnio vai a niygecl ntuiosbsitut ni the cgoalpolrne meculole "
chiwh smaen taht IO hsa a ecnlyig ioutsbnuitst dan thfoerre its luaneb to ormf a doyeacrsn uceurturs.t
Due to lni'gyesc llsma e,szi ti cteersa nsik"k" in eht oainm aicd qunecees. eehTs niksk rae nedeed ot orlteyrcc mfor the rdnaoescy ctr.srutue
Other rean:ssw
y--GlXY si kobnbaec rof nlelocag aplha ia.nch 3 loegnlca alaph icnash lsipra to from rpleit x.ileh nileyGc has no R uprog, linlgwao ofr lxiifyteilb adn fimtroano fo rpleti .xlihe No gliecyn etrepsnv ihts osuiuonnct alinpgs,ri ngrepnviet hte amorntofi fo olaglcen ecosdaryn t.uurretsc
claRel ttah lhhslaeac-ipe dna be-ehtatses era mxseapel fo codsynera s.cetuurtsr iTsh nac eb tuhhtog fo a niatfteinasmo fo het lahap xeihl.
ANorteh way to etg at ti is via i:nnoaitimel
A. goreyhdn onbngdi unwdtlo yaerll ghance ensci eirnhet nnalaie nro leiyncg are la.Bpo r yGl ;tg& laA sonhdtu'l ghcnae ohw plorein si dimedfoi (I mnae ti ULC,OD if eerht wsa a tecisr acrnhinde ro ntho,gmise tbu ont a treag naer )w.Ds iotnnhg to caendtii thta lelogacn erdtangeido is aredtle in ernspseo ot an AA sniibto.tstuu o,slA in the cotntxe fo OI chih(w is teh tgespinnre cmi,ntolap) ew dyrlaae nwok atth het eormlbp sdote'n ahve aythning ot do iwht ,enedditagor orme wiht eth cnehga in /crrft.uusennc itoEtu entHsylo d'not okw.n
r’Hees eon yaw ot r-iiasnepclmeoo-tfes eedde“acrs dbg-roydnhnoe mooi”anrt:f ’Im otn a bgi anf fo hsti ilen fo snienrg,ao ubt tclihlyecna nlaeina sa a idse purog has omer *yhedgsnor fro tlnoeptai doyhgern ngonibd anth elgcniy:
an:nlaie 3—CH
igelcny: —H
S,o eticln”hac,“yl nnaeali louwd pterim oerm rdnhogno-ebyd ,ofioanmrt chhwi ihmgt loawl oyu ot leameniit htat chci.eo
Tath idas, it essem mostal mieibplsos ot eulr otu (iohtwut ryve cacnileht lkogwneed ro osem ovdirpde nexptiameerl tdaa) atht het lhligsty erglar nneilaa sode tno iprami gedhynor bgdionn wtbeene noecgall emusoelcl avi rtsiec l(piast)a rtenfc.ineree nI rmsiepl mrst,e sncei lianane is grealr, ouy wloud khnti htta ti smtu eomswoh tenirfree itwh het dgnygiennh-brood ttha cuocrs thiw eth tedwilp-y iylnceg.
---
S*ircyttl pgka,ensi sit’ not eth mnebru of osehdnygr utb soal eth erntgsht of eth ieodlp htta aecitlaitsf hgedrony :nidgnbo a ynregohd ndubo ot a ltrosgyn tgtoevleecniear ollcumee iekl ierfolnu lilw e”“aparp moer siepitvo ,and h,sut ynhoero-dndbg erom slgnyrot hwit a aynerb nygoex ep(rmodac whit a yneoghrd edcnontec to rcnob,a rof epax.eml)
herturF d:eirnag
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 igthm eb nrvgthnekoii ti ,ubt H ndob mntrfiaoo fo 'asa semka het dscrayoen tcrrtsueu fo eth iotrpne o(clleang ni sith a.ces) eTh lGy ot Aal otnusitbtisu dose surlet in essl H nobd natfoiom,r btu fo vualnddiii 'aas ont beetewn cegoanll ullscoeme t(hta hmtig be omer for aaeruytnrq trstu)ucer
rymPira tuuectrrs = iamon iacd edesucqoaeSrn yecn ettcusrur = tcurusrte dfmero hwti a ienlsg ianmo dcia seeeucqn t(bae lpdaeet eehst, hapal ei,hxl rteaytc rei)T ursuettrc = tpmlueil nacsrdeoy ruteusscrt netagniticr gortthee (teiulpml etba epadtel eetshs kteadsc on top of hace tehor, ernryttQcaa e)ru surecturt = nprotie uustectrr omfedr form idgfoln of all tirayret tsetusrruc ot kema gbniind estsi, ec.t
niSce eht naanlie saw upt ni pclae fo teh ylGniec, the riyamrp rttcuuser saw enlaub to mfor na plaha xhlie esnci alpha lhixe rsrscuteut dnee a parurtalic seucqnee (ygl - x- )y in roerd ot mfor rhnoegdy osdnb to kepe teh xielh e.satlb
awht si naellcog ? a rncdasoey ntoprie .uttsucerr
ewnh uyo remvoe gn,cleiy eth msot aanntubd onaim dcai , frmo the crpoerrsu cleomlue liwl uoy egt a opperr neacsoyrd rrctteuus ? ON
lGy si olr,ap iAlenna si noopnarl adn pcohoydbih.r Msnsseei nreitnonvsocvea u.aiotmnt sThee AsA veah tfndreeif miclceha rpiserpteo hihwc aeld to sedurtdip rotpien lodngif ed(racyson utr.rusc)te Sramili ot lGu - aVl istoutbitnus ni clSkie ellC iesDsea.
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$279$49I hnitk it has siothgmne to do ihtw ieycngl (ued to sit slalm eszi ti nca ift ni ynma scelap erhew hroet mioan sicda acn tno nda enche ti sdivreop tuuraslt“rc eccpt”onsasm to eth lean,gcol i..e tpu a nkki in teh pahal l.)iehx fI nilyceg is misaceldp yb gotnhsiem esl,e I ndot’ thnik lgapc-looner nac mofr tis rtcrcoe cdsnoeary .rctteruus
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