I gdu,refi -iXycnYgle- is llcithcenya cieoensddr a rrpy“mia aimon ciad stueturcr fo a rin”etop cisen eht infdtneoii of a Prmrayi usrettrcu of a tnrpoie si a“ ielanr acihn fo animo .ci”dsa fI uoy msse wthi het riyPmra tcetrusr,u as ni teh suqentoi met,s you tconna form teh yeSradnco urtcutesr fo teh toniper, wchih is emeditednr yb hte gdognyd-oeinhbrn ihwch cuorsc eewnteb het petpdei ceoabkbn, eetdndpnine of eht R .urpsog I oehp hsit dmea s.enes
rmoF iewdikapi: ena“cSrydo steuurrtc is lmayofrl dendeif by eth nrteatp fo egrndyoh dsbno enebwet het nmiao droeyngh dna ybxalrco oxegyn matos ni eth idetepp enbaobkc”. e(iahpssm )imen
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 gysu adn i teuoq form wae/toto1eit-wl/cepdctgltmmebi/iss.rrfthwh/soe4rpouea:oiste02spc.s/n
%"09 evah an itefdanibiel cgeinet inmtuota COL
11A dan LCO 21A
ucs
esa onrabaml lnogaelc sislogcink-rn via a cneilyg tnbiouuitsst ni teh ergoonclapl eluoemlc "
hcihw mnsae htat OI ahs a egncily stsiuitnubto nda erteofrh sit eunalb to rofm a edrysonac csre.uturut
eDu ot nigslc'ye llasm es,iz ti ectasre s"in"kk ni hte onima cdia cuesq.ene ehsTe nskki rae enedde ot ctyrleorc mrof het orycndsae ucu.ttsrer
erOth :nwsasre
X--yYGl is ekbnaobc rfo acgoelnl ahalp naci.h 3 neocalgl pahla ancshi plsira ot from ilerpt ehix.l lcneGiy ahs no R pu,gor ollgawni ofr ybxliieltif adn fntmiooar fo tpeirl exi.lh No ligenyc nprveets tihs notnicsuuo rnap,gslii envgtrnipe het iortfaonm fo olgcneal oydrnacse .urtutsrec
aRlelc htta sheph-lcailea nad eeshsbt-tea rea saelmpxe of dyeosnrac re.ttucrssu hsiT can be thouhtg fo a inmnoetatfsia of eht aphal .lxhie
hreAtoN way to tge ta ti is aiv oeaitilnmin:
.A ygornhde godnnib tluwndo rlaeyl ceanhg encis rinhete nialnea onr gcenliy are B a.olpr Gly ;tg& laA tnlodshu' heganc how lniepro is eifomidd I( name it LUOC,D fi rethe asw a cetris enrnchida or omte,sighn btu ont a tgrea .Dne) rsaw ntoingh ot aetidcin thta lelgaonc teridnogaed is edrtale ni enossrep to na AA otnsiiuus.btt lA,os ni het ctxteno fo IO w(ihhc is hte ringpenets lpit)omnc,a we dyeraal wkon htat eth blermpo etndos' ehav htngayni to od hitw rdnte,iaeodg omre thwi het nahcge in .rEo n/rucfisttuucnte otHlnyes ot'dn no.kw
esre’H neo ywa to soliiar-teco-fesmnep csrede“ade nn-obhrdodyge onafmir”:ot mI’ not a igb anf fo ihst eiln of nrgeonia,s ubt acentlylhci inlaane as a sied pogru hsa erom nse*hgyord fro eialottpn dghnorey iobndng htna icnlyeg:
ian:enla CH—3
engic:ly —H
S,o “”hitaleccnyl, lanaeni owldu reimtp emor -yreddgnonboh ,moriafton hhicw mihgt olalw oyu ot taimeline ttah .cchioe
tahT i,das ti msese smlota peosmlbisi ot rule tuo twtuo(hi evyr cehitnacl klgoeedwn ro smoe ivrpeddo elienapmextr )data atth eht sghllyti rgaelr naelian sedo ont aiirpm doynhger dibngon bteenew aoeclngl ucoslleme vai rticse ia(stal)p .eeneetcrfnri nI rlmsepi ertms, sncie anlaeni si lrerga, oyu luwdo kihnt tath ti utsm oehosmw etreferni htwi eht eogdhnibn-ndygro htta uorcsc tiwh het -tdiwyple cilgyen.
---
Sl*tyctir pniakegs, si’t ont eht urbemn fo ehryodsng but alos het hgrtnest of het iodelp hatt aieasfilctt hdegnoyr oibdnn:g a rnoydegh bnudo ot a lrtgynos eoilgntcateever eelcomlu ikel liruoenf wlil a“a”prpe mreo etsvioip ,nad ,suth -hnbydnedoorg moer orsnyglt thwi a neyrba yngoxe c(oeadpmr hwit a yorgendh tonceendc to bnc,rao ofr lme.xpae)
tuhreFr d:neragi
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 hitgm eb ikenihgrtnov it ,tbu H onbd mfiraonto fo sa'a mksea het ydrcoesan erttsuucr fo teh neoptri o(lgaenlc ni siht ae.sc) eTh lGy to alA usubtttinsoi oesd etsulr ni essl H bdno ,itaoromfn utb of ldiiaiduvn asa' ont eewbent eogcnall seullmceo th(at mhigt be omre rof reraaunqty r)setutcru
yrrPmai uttcurres = manoi dcia nqScsaeoyuceee nrd csurterut = uerttucsr odemfr ihwt a leinsg inmoa aicd uceesqne abe(t tapleed ts,hee halap xihle, earcieTrt yt) rtuerctus = leimtpul daencosyr tcurrusets ineatcngtir gretohte l(uemptli btea dtaeelp etessh edtaksc no pot fo chae to,hre ec rueyQara)rtnt tcrruesut = rpnteio ertsutucr oedmfr mrof gfidlon fo all yrrtetai rtucerutss ot mkae ndbigin esst,i tc.e
eicnS hte nielaan was upt in celpa of the ,Gclenyi teh rmpriya sretuutrc wsa luebna to rofm an aphal eixhl scnei aplha hixel euurctstrs dnee a arriualctp ceenusqe y(lg - -x y) in rdroe to morf hnorgyde ndosb to peke het hixel sa.telb
awht is llgoneca ? a soraecdny reonpti tururetcs.
whne oyu vmoere ye,igcnl het mots atuabndn naimo cida , ofrm the uerrropsc uleecoml lwli ouy teg a errppo sreacyond trueucsrt ? NO
lGy is par,lo enlainA si lonparon dan y.crdooibhph eMensssi acvvsreontieonn .tumantoi eThes AsA eavh ffetiendr ecamlhci eptrrspioe hhwic eald ot uesrdpdit ertpnio gdilnfo racosye(nd su)cre.ttur irilmSa ot Gul - lVa bisiounttstu in kciSle lelC si.aesDe
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$279$49I tnkih it ash osntmgehi ot do ithw ignecly u(ed ot ist llsam zesi ti acn fti ni anmy eclasp erhwe htroe ionma adsci can not dan cehne it sirvpdoe ls“ttaucrur n”aspccmetos to het oacgleln, i..e put a kink ni eht phala i)helx. If gilnecy si impasldec yb nmogsihte ele,s I o’tnd nkiht nlclaeoropg- nac fmro ist tcrcore sdyranoce euscr.rttu
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