I d,ugerif gnXle-ic-yY si hlacelynitc senrdcdeoi a pam“irry moain dcia eutsucrrt of a tp”irone encsi teh ndeonitifi fo a irymPar tceuurstr fo a peoinrt is a“ lnaeir cinah fo amoin i.da”cs If oyu ssme tiwh het yiamrPr utctesru,r as ni teh eotnsiuq et,ms you acnnot mrof het enaScydro sturuerct of het pnreoi,t hhiwc si merdntdeie yb teh rndggyobnnh-iedo hhcwi rsoucc eeewnbt hte eppited eocbnkba, nineneedptd fo the R upgros. I hpeo isht deam snees.
Fmro pkwieiiad: oednary“Sc tertuscru is amrlolfy feednid by teh aperntt fo enorhydg sdnbo eeentwb eth onima ohnedgry nda oxbyracl xogeyn tamos ni eht edtiepp obckbena.” ampsi(hes min)e
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 suyg dna i tquoe from irn4oge.lsw2afssi.sopoew/pt1/udlicthett/0/imehe/eba:reowtsom-psctrct
9"0% aevh na iftaebldieni cnigtee omiatntu
OCL 1A1 nad LCO A12
uac
ses amborlan conllega irk-gcilnonss iva a ignelyc ssniiouutbtt ni hte nlegpcoalor coeumlel "
wcihh sanme ttah OI sha a nlgicye utbuiisntsot and ertohfer ist ubanel to mrfo a ycsrdeoan s.trutucreu
ueD ot gle'icsyn mslla i,esz it saeertc nk""ski ni the animo idac ec.qsuene eThes niskk ear deende ot cctoyerlr rfom het yecroasdn rs.trectuu
trOeh enswr:sa
GY--Xly si beakbocn ofr nleocgla alhpa .china 3 ocnllgea hlaap csihan sprail ot mrof tierpl .iexlh leyincG sah no R pru,go iwnloalg fro eillfbxytii dan ofnitmrao fo ipletr .lxeih oN elncigy tnrvpsee shti cnuuisntoo rnpsilagi, pvneeitrgn teh ntoaroifm fo olacgnle ydnosreac tuc.returs
lceaRl ttha sc-aeiahphlel adn s-hteetseab ear xaselepm fo raynsdeco strc.rtuues shiT cna be tgtouhh fo a aftinanometis of eth alaph ile.xh
ehAoNtr ywa ot get ta ti is vai ne:limtioain
.A yndroheg nobdign uwnltod llaeyr ancgeh sienc ieernth ninaela nro lcngeyi rea rBalpo. lGy ;gt& Aal dthnuso'l hcnaeg who nrpleoi si mdiefodi (I eamn ti ,OUDLC if eerth wsa a esitrc anenhrdic or ,emishngot ubt nto a etgra a)n.s wrDe gtoihnn ot aditicen hatt ecloangl egdradeoint si erldeat in sonerspe to an AA uiuosni.bttst l,Aso in eth etnxoct of IO c(iwhh si hte etisnpgern noi)apclm,t ew yrleada ownk ttah het orlembp tdo'esn vhae nhtygain to do with natedie,rodg orme thwi the nhegca ni tuiunEc r/.srunotfcte eHyonstl dtn'o k.onw
s’eerH oen way to -pfootiselrnease-cmi as“ecreded dnnybogrode-h rmfoiao”nt: m’I otn a gib anf fo itsh nlie of ernngisao, btu ctanychllie lenaian sa a deis gorup hsa moer nygd*ehrso for olitptean gndeoryh bignond tnah lgeycin:
:ennaial 3CH—
cenilgy: —H
,oS hlccn,ayie”tl“ ninaela dowul piermt mroe ghndybrdno-oe o,oafmnirt ciwhh tmgih wlloa you to ianeimelt hatt c.cieho
htTa ad,is it msees tamlos imsispbloe to ulre tuo wt(ituoh rvey hcatlcine lkogdewne or mseo ddrieopv teielepxanmr aa)td ttah eth sllhityg rrlega alannie edos not iiarpm eygdhnro nnbgdoi netbewe econllag luecmlseo vai ecsirt iaaplt()s eir.nneeefrtc nI msrlpie rmet,s ceins naanlie si ,rlarge yuo udlwo knhit ahtt ti must woheoms nrtfeerei thiw eht dnebdo-oggnynrhi atth coursc twih the diely-twp iencylg.
---
*ryttiScl kipsnea,g t’is ton eht rnemub fo ehgnodysr utb aslo the nhtstger of teh lidepo ttah aiietcfltas oghdnrey n:ignbod a ordgynhe nduob ot a nlysrtgo etnlreavetgoeic cleleumo elik rnliefou lwli r”ppaae“ omer itesipov n,ad ut,sh hrneyondgd-ob oemr gtsyolnr ihtw a arbeny ognxey ardm(oecp wiht a ernyodgh nocntceed ot ncbo,ra ofr .expmae)l
hFeutrr rdg:niea
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 mihtg eb ognknhveriti ti utb, H odbn fmoraonti fo 'asa kaems teh nscydreoa tutsrceru of hte npeirot (lacgenol in tish c.e)sa Teh ylG ot alA niustitubsto osde tueslr in sles H donb taomoinfr, ubt of ddaiviiuln sa'a tno eetnewb elongalc mlluceeso taht( gihmt be ermo rfo nraryuqtae )currustet
rriyPam ruusetrtc = ionam aicd odaneq ruseceyenSc cretutsru = etsurcrut roemfd whti a gniesl imnoa daic usceqeen tb(ea etaepdl s,tehe aahpl h,ixel aecTtyeritr) erstrutuc = pimtleul oaecsdynr csuretustr nagectirtin teteohgr lti(melup ateb aledpte hstees detcsak no top fo ache hetor, er tcerayrtaun)Q crttrsueu = oieprnt ruteutscr demrof rmfo dlniogf of lla trieryat ustsutrrec ot kmae bigndin ist,es ce.t
Senic teh enlinaa saw tpu ni apcle fo hte Gc,ieyln hte rriamyp rcesuturt saw eabunl to rmof na aahlp elixh nceis aahpl hixel crrussutet dnee a riptarlcua eeqsenuc yl(g - -x )y ni rorde ot romf dyrehong dbnso ot ekep het ixelh stba.le
ahwt is alclnego ? a yecrasnod enirotp rterut.suc
hnwe uyo vmroee glyie,nc hte most nbaautnd niaom caid , omfr teh srcrpuore olcuelme illw uoy etg a eorprp csanryode crsurtuet ? ON
lyG si olpar, eAlanni si oraolpnn nda .odhpyohbrci ssMesein vreneconvstnoia tin.uaomt hTese sAA veah dfenrfeit lchiceam sperriopte hciwh aedl ot urdpitdse orpinte lignofd dseon(rcya )rsuecrtt.u rmliaSi ot uGl - Vla ttibuosisntu ni Selkci Cell .esDaies
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