I fgder,iu -gYciXy-eln is ltlyneaihcc oeincdsdre a mrr“paiy nioma iacd rcuetrsut of a o”tnrepi nscie hte nditnifeoi of a ryPrmia teuscrtru of a nroteip si a“ nrelai chnai fo aimon a”cdsi. If you ssem wiht het mrParyi urcrst,uet sa ni eht notuqesi e,tms you aontnc form eth derynSaoc csurreutt of teh etrinpo, ciwhh is emdeeirndt by eht iggehndbnnro-oyd hhciw ccosru ebewnte eht epitdep kcbnoabe, didnpetneen of hte R u.orgps I heop ihts eadm es.nse
Fomr iipikdwae: “aSdceroyn uetrsctru si fmallroy eiefndd by eth tpatenr of gednyohr sbond tbeween teh aiomn drohygne dan xcloyarb gyoexn tsamo in teh dpepite nebbacok”. smepiahs( n)emi
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 syug and i uteoq rmfo toh-lmoa/e/ftewir.lgotrptwi/nemos.d2ortci:/saehctsiwpeb/s14e0ptcuses
"0%9 avhe na entibldaeiif eicengt aoumtitn C
LO 1A1 nda LCO A12
usse
ca naaobmlr clgnlaeo nisnkorlc-sgi iva a cynielg tbontisitusu ni het oglpnalerco lumeeclo "
ciwhh emsna atht IO ahs a nelgcyi tbonsusuttii nad erhfteor tsi enulba to rfom a racoyneds uu.reustrtc
ueD ot gyl'ncise sllam ,eizs ti ateescr n"kik"s in het nomai ciad uq.ncesee eesTh nsikk rae nedeed to rorlectcy fmor eth dcasoyren trutcs.reu
thrOe nreas:sw
-X-lGYy is onbkcabe for oelngalc aplah ihan.c 3 neogcall hlpaa acsinh rsalpi ot fmor triepl i.xelh Gecinyl ahs no R gp,uro nlgwilao ofr bfliyexilti dna otrifamno of pliert hxl.ie No eilcnyg eetrnvsp isth tunsuoncoi pisgian,lr neerpngvti eht tfiamorno fo ncogaell dcyensroa rtctsu.ure
Rclael ttah hea-ahillceps dan s-tshbeetea rae eapsxeml of ocensdayr crtsuret.su hTsi anc be htohgtu fo a aiefatsmniotn of eth hapla .xielh
rANeoth yaw to get ta ti is vai t:neoinialim
.A yongdehr ognindb ndlotwu llyaer nchaeg encsi rntehie neliaan onr lgiynce ear .lBo rap lyG t&g; aAl slt'nhoud cgehna woh erpnloi is feodimid I( enma ti ODC,LU fi hrete swa a sirtec crenhidna or eot,gsnhmi btu ont a getar wDsrae.n) gtnihon ot cinietad taht noeaclgl dgretoieand si aeedltr ni srsnepoe to na AA i.iuossttnbtu s,loA ni eht etntcxo of OI (hchiw is eht itgnnepesr nom)lta,ipc ew lyarade wnok hatt eht relpomb sodte'n veha hyniagnt ot do tihw ni,todaeegdr mroe wiht the hcnaeg ni cctsrtiuEu.turnnefo/ Hntlesyo 'ondt wo.kn
s’erHe one awy ot natcrselmfe--ioesoip “srdaeedec b-doyhgdnonre n”tomar:ofi Im’ nto a gib fna of sith ienl of ons,anierg ubt hcenaycltli ainenal sa a esdi gprou ash mroe dgoysrhne* rfo nitptolea nrohgeyd igondbn tnha gnyicle:
ilan:ena —HC3
lgiy:cne H—
So, a”,cillnct“hey ailnnea dwuol imretp emor o-hnndygreobd ratnio,ofm hihwc itmgh ollaw oyu ot eiltnaime taht occh.ie
tahT di,as ti messe soamlt slsiiempbo to uerl out t(iowhut eryv calenhitc wgeolednk or meos vdripode ernexplmaeit atda) tath eth yhgtlsli alrgre nianlae does nto miripa nhoeydgr ingdobn ewetnbe galolnce lceeoslum iav rescit )itsp(laa .irreeftencen In prsmile smr,te nesic nlianae is alre,gr uoy luwdo knhti htat it utsm moosehw etiernrfe twih het ngerhdo-ndynbgio ahtt uoccrs thwi het yewipld-t celgyni.
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yctrilS*t sep,anikg sti’ nto eht nmrueb fo hosyenrdg btu aslo hte ngtshter fo het ioplde ttah etscafiltia rdgoeyhn :gbonnid a rodgeynh dobun to a ysrltong ginlvterectoeae lloceume kiel nufirole wlli pae“”rap mreo tivoeisp d,an sut,h engon-dohbryd mero lorygtns hwti a ebayrn nxgyeo ed(ocmrpa tiwh a ehrogndy cntnodece ot nborc,a rfo )aml.epex
rFtureh gniared:
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 htimg be einronivkhgt it b,ut H ondb mfiaootnr fo saa' meska eth rnycoesad tcrsrtueu fo eht tinepro nlel(coga ni ihts a.cse) The lyG ot Ala iuitntosbtus dose utrels in sesl H odnb ,omtfoniar ubt fo vaidiliudn s'aa tno eewntbe gnecaoll oelsmluce tt(ah might eb orem for ryaeqarunt sctreurut)
ayPrrim curusettr = oamin caid eaueeccqend soySnr srcetuurt = restucrut dorefm twhi a seglin nomai acdi cueseqen beta( teedpal sht,ee hpala lhexi, t r)Ttreyeiac trsercuut = ullpmtie onsaredyc euttusrscr rtinnticage eothgtre u(lliempt eabt eldaept tseshe dscekta no otp of each o,etrh tr)yartnQeeracu srttcuure = onrtepi rturcteus orfemd form lndiogf of all treitrya tcssurtuer to meak nbdnigi tss,ie ec.t
nSice teh eanialn swa tup ni lepac fo hte lyeGc,ni the miapryr euurtctsr was lnbeau ot rmfo na aalph xhlie ecsni apahl lixeh suestcrrtu ndee a plructaria ueqecnes gy(l - x- y) ni roder to fmro yenhogrd sonbd ot epke hte lihxe sela.tb
what si ceonlagl ? a donsyrcea itonpre tr.uteuscr
ehwn yuo rmoeve ycnigel, the mots ntnudaba manio cdia , frmo teh reuoprcsr elmcluoe wlli you etg a eoprrp ornadsyce resctrtuu ? ON
lGy is oar,pl eaiAlnn si aolponrn adn ocdrpyh.hobi ssnisMee oaitecrsvenonvn itanot.mu seTeh sAA hvea ditferenf ielaccmh pertorespi hcwih aedl ot idrdpeust perinto fdinlgo odnacesry( re.u)stctur ilimrSa to ulG - alV tiobuntstsiu ni iceSlk lCle eDsisae.
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$279$49I nthki ti ash goinstmeh to od hiwt ngiylce d(ue ot tis lslam izes ti cna fit in anym pceals wehre eroht omani dcsia anc tno and enhce it ivoserpd utrcrl“tasu asopesmnctc” ot het ,golelanc ie.. put a kkin in eth aaphl e)ixhl. fI geynilc si lscmdpiea by nhtgosmie e,els I dnt’o khint oenargclopl- cna fmro sit recrcto ceaornsyd st.rurcute
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