I egfudi,r lig-Y-cXney si nlealychcit dcsneoider a aim“yprr naoim daci etuscutrr of a preiotn” secni teh tieiindonf of a miyrrPa rttuursce of a rneipto is “a airnle hcian of amino ”iasdc. fI yuo mses ithw teh rPryima ucesu,ttrr as in eth qtsnoieu mest, oyu anotnc omrf eth Sycnrdeoa setrrcutu fo the pireon,t wihch is eedminetdr by hte beoydghgion-rnnd hwihc cscoru wbneete hte ietedpp abnkoceb, ienptnednde of eht R usr.ogp I epoh tshi deam se.nse
morF ewidikipa: ercado“Sny trtesucru si ayolfrml efddnie by eht antptre fo eognhdyr odbsn enteebw the mnaoi rnedyhog dna abroylcx goxyne mstoa in hte ppdetie beanockb”. ss(iehpma emni)
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 gusy adn i uqeto mofr a0f:s/sdo/l2scmpmg/l-et/s4isr.1banti.owiicptoptrttrwueehswee/ooethec
%0"9 ehva an bftenidieial iectgen amtouint OC
L 11A nda OCL 2A1
sasce
u alnoarbm canoellg iknsslrgc-nio iav a nlygice oittubuisnst in het lrcglaoeonp lueloemc "
whhci amnse that OI sah a nlygcie istiusntbout nad erhrteof sti eluanb ot romf a neysdcaro usrtcurteu.
euD to ny'gielcs mlsal izs,e ti sreceat n"skk"i ni het naimo acid seeceu.qn eeshT knski are neddee to clroctrey fmor eth scaroyend sructetu.r
eOhtr ssnwear:
l-G-XyY is ncbbokae fro ocellgan aplha nh.iac 3 gleoclna lahpa nacihs siralp to orfm pretli xielh. neylcGi ash on R upg,ro lioglwan rof eiflblixtiy dan omafintor of petirl .hlxei oN lygniec evpsrnet hsti ocuonusitn lipragin,s pretvnnegi eth oatoinmfr fo lgoncale rncdosaey ur.tuerstc
lecRal ahtt hl-shiacaelep and e-tesbhsate rae mpsexlae of dansryeco tscu.urerts ihTs nac eb huottgh fo a tfmaninoaetsi of eth phlaa he.lxi
ehtoArN wya ot get at it si iav o:anleiinmti
A. egoydrhn bnogndi woundlt ayerll cghnae isecn eritneh ealnani nro cngylie era Bo.lapr yGl ;> lAa ldoutsh'n ahnceg how nplioer si idmdioef (I mean it LDO,CU if htere wsa a itscer candirhen or gihtmsne,o tub ton a tgrea .aws)nDre igtonnh ot ectandii ahtt leagconl ietoedgnadr is rletaed ni neroepss ot na AA bsuoiniutst.t l,oAs ni the toxcetn fo IO w(chhi is eth pigsnetern )oclmpiatn, ew dalyrae nwko hatt teh rpoembl teson'd aevh ngtyhain to do htwi rdaeoi,nedgt mero wtih teh nhgcae in .oerctfE/ic tturnuuns netyslHo 'dtno nk.ow
’reeHs one way ot -teeen-rcipaoliomsfs serededa“c bo-ynrgdenhod matoi”fn:or Im’ otn a gbi naf of shti line of ,eongsanir btu lanhlcyteic aanlien sa a deis porug sah remo rengdho*ys ofr tanpoeitl nodgyher dinbngo tnah clgyein:
ilna:ane C3H—
nc:ygile —H
,oS ”l,icnc“lytaeh iaalenn ludwo empirt moer rbnegdoyhond- i,oaotnmrf whhic ghmti lolaw ouy to iatinleem hatt eiccoh.
Thta ais,d it semes omlsat soibliemps ot rleu uot iwotuh(t eyrv tcaiecnlh edknlwoge ro esmo verpddio rpeietnxemal aat)d htat eth lygslith rrgeal nialnea dose ton apimri ryhnoegd noinbdg nteeewb cegllaon oemselluc avi rtesci aa(p)tsil tener.fcireen In pimrsel ,rsetm sncei elinnaa si rrgea,l uyo odwlu nkthi tath ti msut oohmwse erefiretn tihw hte egbnhrdydnigoo-n atht orsccu hiwt hte dpteyiw-l geynicl.
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cr*tltSyi sgenpak,i s’it tno hte mrbnue fo edhnorsgy utb lsao het httrngse of the dpileo atth saittlefica rnoyghed bnigdo:n a eyodrghn dubon ot a lrtsgnyo ceneirlevtgeaot cmloeelu lkie ouelfirn lwil a“a”rppe moer esoiivtp d,na hsut, nrynodbod-ehg mero olrystng whit a ernaby oxengy oard(pecm whti a rygehodn odectnnec to na,cbro fro elx).maep
urtFher id:rgaen
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 htgim eb rioiehnkvgtn ti ut,b H dobn aiootmnfr of asa' esmak teh osyrdncae tercuutsr fo the tneproi llgnco(ea in sthi )ecas. Teh yGl ot alA ubtiintuosts edos rlteus ni ssle H obnd ,motnfraio ubt fo iduaviindl 'aas ont ebewent caglolne smeluloce ha(tt mihtg eb mero rof uyaaretrqn te)turrsuc
maPyrri ttsureucr = ianmo cadi eqyeu noSdrcanecse tectuurrs = esucrturt foemrd hwit a islgne inoam icad cnqeeues btea( aetedpl hst,ee ahapl hei,lx r tcyriae)teT rsetucrut = muiptlle ncsedyrao utcsrtsreu artitienncg ortheetg emptulil( eatb edtplea thsees aktedsc on pot fo ceah ho,rte un)rtrrteeyaQac etucrstru = oerinpt ctusrtrue efodmr romf dgonfli fo lal tryriate trusuertsc ot make nibding ssit,e .etc
inceS het elinnaa wsa tpu ni eaclp fo teh elci,nGy het pyrmari rtcureuts asw auenlb ot ofrm na halap xhile ncise ahalp ilxeh ctrssertuu deen a caairurptl eseuecqn y(gl - x- )y ni dorer to mofr dnygreoh bonds ot epke teh lhexi etbs.la
twha si naelgloc ? a aysdonrec eprnoti rttuuesr.c
enhw uyo mvoere yneil,gc hte otsm nntabuad animo caid , rfom the orrpeucrs eluoecml illw ouy gte a rpreop decsranoy ertustruc ? NO
yGl is l,paro Aenlina si rloanpno nda obhhypcoird. iseesnsM reaosteocnvinnv otnaimu.t eseTh AsA veah ertfidefn eilchmac etorpipres hhciw leda ot epstrddiu ontpire flodgni cyrena(sod retut)crus. iraimSl ot uGl - alV bsinoutttius ni eclkiS eCll eDie.sas
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$279$49I kihnt ti sah heitnsmgo ot do thwi nlgyiec d(ue to its smlla eizs ti cna fti ni many aplsec wehre etrho noiam dicas can not nad hceen ti siovrdep sutculr“tar mstec”oancps to the anlogc,le ..ie tup a kkni ni teh ahalp eh).ixl fI eyngcli si cedmipals yb gnhseimto es,el I ’dtno inhtk apclroeog-ln can fmor ist orecrtc caeysrdno .tsurcuert
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