I ,grfudie lc-yne-igXY si ynciechtlla dsndicoere a p“yrrima amion daic tcrusruet of a ”epriotn senci the ntdfoiniei of a aiyrPmr retsuurtc fo a ponerti is “a nralei ichan of imoan ac.dis” fI yuo esms hwit the yParrmi rtucur,ste sa in eht uqnoitse ems,t yuo tnaocn frmo the Snedarocy uusrctetr fo het ,reitnpo whchi is irmednteed yb eth ghndeinry-odognb iwhch sorccu beteenw teh ptpiede bnoakebc, nndpneditee fo het R por.sgu I pohe htsi dame sese.n
rFom wipidkiae: rceSodny“a strctueru is ylrfomla defdien by het arnttpe fo herndoyg dbosn tenwebe hte manio enyhdogr and yolrxabc nygoxe stoam in hte ideeppt oenckabb.” shps(eami e)inm
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 gysu dna i uoeqt omfr i/tcoiels/sntmews-.cwoeecp4rus/lat0tom/p/eofar1shhgw.otesiptid2treb:
%"09 veha na dfeliaeinibt ctegine tntomaui OCL
A11 and OLC 2A1
saeucs
aormalnb lnlceoga ngs-roknilsic vai a gyilecn utotiusibstn in teh ceorlngaolp oeucleml "
hihcw nmsae hatt OI hsa a eygincl ntsitiuubost dan reoerfht sit enuabl to frmo a enoydsrca uturesc.tru
Due ot gse'cynil lalsm e,izs ti ceseart i"ksk"n in hte nioma aicd n.euqesce Thsee kskni rae deeedn ot leyotcrcr rfom het ranoecdys stutecurr.
rehOt a:swersn
Gly-Y-X si ecknabob ofr genlocal palah hcai.n 3 lonceagl lahpa sichna islapr ot orfm pltrei e.ilhx elcyGin sah on R ,uorpg ilganowl rof xliieftlybi dan itaofmrno of eplrti x.hile No ilnyecg tsveeprn itsh onnciouust spiian,lgr inpveergnt teh mtoafroni fo lcagnole scnorayed ute.tucrrs
elRacl ahtt iaelphlasech- nad thsae-eetsb rea xslapeme fo yeanoscrd ret.susruct shTi can eb ohuthgt of a taftoiiseannm of het paalh xlhi.e
NhrteAo ayw to gte ta ti si iav o:leinnmtiai
A. dnyrgheo oibdnng nwutdol reyall gnecah csien thnieer laanien ron glyenci rae . lpBaro Gly g&t; alA oudl'thsn aehngc owh nrpioel si idfeomdi I( maen it UDOCL, fi reteh swa a ietcsr enniadcrh or smgehi,ton tub otn a rgate )anw esDr. htoning ot dnieicat hatt nlaeclgo eadtodirnge si draelte ni eoespsrn to an AA .tsoutniibust oA,ls ni the xtncteo fo IO wihc(h is eht rnieepgtns cpaot),ilnm ew ladreay oknw thta eth pbmrelo ntd'oes aveh hantgyni to do hwti ntgaodrdee,i rmeo twhi teh gehnca in uu u/frinoncectt.trEs lynsHteo tdo'n .nokw
r’eHes eno way ot soeiaemtifn-lrse-ocp dea“sdcree ornegydobhn-d om:fitr”oan Im’ ton a gib nfa fo tsih lien fo n,nrsaeiog utb ncctlilaehy aainlne as a ised ouprg ahs oerm d*sreyonhg rfo tnoelitap dghenroy innbgdo athn neilygc:
a:nliena 3CH—
elcn:giy —H
o,S c”aenhct“yl,il ialnane wodul prtemi more hgobdyn-deron rtoimfao,n hwihc ghitm lwlao oyu to imtinlaee tath ihc.eoc
Tath dai,s it esesm asolmt issmieoplb to rule out i(huwott vrye hitnccela ewdlgonke ro moes dierpovd iemltxrepane taa)d tath teh hyltlgsi lrgrae alenani edos otn riaimp ognydher bndngio eetwben llcegona oelemclsu vai srceti lp)iats(a rnifeencee.tr nI smliepr srtm,e enisc aalenin is arl,reg uoy ludwo inthk tath it tmus soewmoh iretenerf thiw eth nobrnedinohd-ygg htta ccsuro thwi hte iyewtpld- leyngic.
---
*Scyltirt eignk,pas s’it ton eth mrnbue fo yhnrodesg ubt oals eth sthnrtge fo hte lopied hatt citaafeilts ngeohdyr gdo:bnni a dnoegyhr uobnd to a ytrlngso cgvelniotrteaee ecmelluo eilk uroielfn lwil paepa“r” oerm ipeovsit ad,n ,suth d-ehronbngdoy reom oltnysgr with a baenry xenygo e(damcpor ithw a gohndyre etnoecndc to ncr,abo for .epaem)lx
ruheFrt ndaie:rg
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 hgtmi eb neotgvkihirn it ,but H ndbo taoimrnfo of a'as seakm teh dyescorna etcrrstuu of hte epintro (gnolecal in hist c.)sae heT Gyl ot Ala titibunosust dseo uetsrl ni sels H ndbo rian,tmofo btu fo idlundavii 'saa ton nebtewe conglale mselluoec (htta ihtgm be mero rfo uyrataenqr urtusecrt)
Piramyr uttrcsuer = ioman daic s eSnqecadoreeyucn tturercsu = tceurutsr orfdem with a lnisge amino acdi eecuesnq b(eat edlpate stehe, lapha xlh,ie tT)cateyrrie euurttcsr = ltemulpi rdoceyans crteursust gantrtcinei ohetrteg u(ietllmp tabe aptedel shtese cestakd on pto fo ahec e,thro r ueaQ)nyractetr cursertut = rnopeit rctreuust ofremd omrf gdnfoil of lla eyartrti reuscutrst to eamk ngnibdi iest,s c.te
ineSc hte alienna aws tpu in lecap fo teh liy,ncGe the mrirpay tutrerucs wsa ebunla ot rfom an ahpla hxeil icens hpaal ilhxe urcusrestt ende a clpaatiurr esucneeq gl(y - x- )y in dorre ot fmro honydger dobsn ot eepk hte hxlie betsl.a
whta si lclagneo ? a rnaeodycs irnopet u.trrceuts
wenh uyo mrevoe nyglc,ei hte omts unadnatb nmioa iacd , mfro eth erpucorsr cleumelo ilwl yuo egt a rpeopr rnyeoascd cretrsuut ? NO
ylG is r,olpa eliAnna is ronlnopa dan .yohbripdohc nsesseMi novtscrenonaevi umn.titao Teseh AsA vhea fnditrfee clacemhi rpierotpse ihhcw eadl ot edtprusid rteipon fgdloin coe(ydarsn crrsuet)tu. Siiralm to uGl - Val oibttsstunui in kSeicl lCle sDei.sea
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