I frgeui,d yclg-XYen-i si ihtyecllnac odcdienres a “ripmray amnoi caid tcrusuret of a pe”itorn cisen het iioetnifdn of a arryiPm tsucturre of a iontper si “a lieanr cnhia of aniom .”adcis If oyu essm iwth het irramPy t,suurrcet sa in teh sqiuotne ,etsm uyo acontn form hte dnreaoycS euctsurrt fo hte tpro,nei hihcw si dirtneedme yb eht reoynnoggbhd-nid wichh cuorsc webeten teh peipetd bckeonba, ddtneeennpi fo eth R pr.sogu I opeh ihst edma .esnes
rFmo wieipkaid: odSe“rycna cretuusrt is malyfrol dieedfn yb eth terpnta of rengdhyo osndb wtneeeb the nmioa yreonghd adn oybclxar onyxeg stamo in the pteeidp okenbacb”. ph(siesam mn)ie
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 sguy nda i tqueo from wc.o/e-ist/:lui./ac/ethochpmosoos2ftnterr1awleiwss/degt40pbseeiptmtr
"90% evah na ibneletiadfi gteenic itutmaon
LOC 11A nda OCL 21A
ucs
sea nbmarlao olcglena ksgncni-risol aiv a ygnlcei uiutsnibotst ni het nclerolapgo ueoclmle "
hwhci ensam atth IO hsa a gnyicle oiubnuitsstt adn etrhoefr tis unbela to form a doaesyrnc uuttrerc.su
eDu ot isne'ylgc lasml ize,s ti esrteac kinsk"" in eht aionm icad qs.eneuec Teesh snikk ear dnedee ot creycrtol mrfo hte rodacnsey .ctsurreut
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eallRc htat lhp-lshaceiae and a-stbetshee era emsaxelp of rsoyanced uurrts.ects Thsi cna eb hutothg fo a eiftmnoinsata of hte alahp xhl.ei
oNehArt ayw ot egt ta it si avi imiaonine:tl
.A enyhdorg nidogbn wlnotud ylelar ncgeah escin ehnirte enanail ron nyiegcl rea .laB orp ylG t;g& lAa nohstu'dl encagh owh pnreoil is ieimdodf I( mena it ,OLCDU fi etehr was a critse eninhdacr ro geios,nhtm utb ton a taerg weDa)rsn. nnithog to dinaetci ttah leogalcn egdiatenrod si atelrde ni sesnopre to an AA itsoin.ututsb ls,oA in teh ncxoett fo OI hihwc( si the itpgernesn ,cia)tpmlno we aylarde kown ahtt eth pblrome d'entos ahve itnyangh to do wthi dangeo,rited meor with the aegnch in s/fuinrucot tenuE.rtc nstoeylH dnt'o wo.kn
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nnailea: 3HC—
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oS, ynt”“li,lacceh naniela oudlw tpirme reom nhdengo-rdboy f,iotramon wcihh hitmg owlal uoy ot intaelime tath ecoih.c
taTh sd,ai ti smese tomlsa sboispmile ot rleu uot uo(wtiht ervy enctilach elewkdgno ro seom vdoierdp aximreenlpte t)ada ttah eth lthgsliy lrgrea lainena sedo tno riampi geonyhrd inogbdn tnebeew elcaonlg luoemelcs avi etrcsi )ia(tpsla ce.ntrirfneee nI rmsilpe terms, iesnc eiaalnn is eralg,r yuo dwuol ihntk atth ti utsm emwsooh enftrerei iwth het -gryodnohingbedn that rocusc with eth itelwp-dy igyclne.
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*ityrSltc igknp,sae is’t tno eth rneubm fo grynhdoes tbu slao hte herngstt fo het lepodi hatt aclaetsiift ehnyrdog odnnb:gi a egnohryd uodnb ot a tognlrys lceteaeivrgotne ulclmeoe eikl iurlfnoe lwil “p”arape reom oisitepv ,nda t,suh od-ndrnebohgy ermo ygosnlrt tihw a anebyr gxyone damoc(pre wthi a odyenhgr eenodcctn ot oabncr, for )ep.exlam
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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 mtigh eb rgintheknoiv ti tb,u H odnb otfnrmaoi of a'sa kesam teh oadecynrs tteuurcsr of eth epirotn ec(allgon ni thsi ecs.)a Teh Gly ot Aal utustostinib deos sutrel ni slse H bdon rt,mioafon btu fo ivdliundia aas' ton nwetebe nloacegl uolecmsel thta( mghit eb more rof arrtyuaneq rt)utcures
rPymiar rtsucerut = omain cida uoq aceyseencrndSe utcsruert = turcretus oedrmf whit a seglni inoma idca qeucseen teb(a dltpeae ,ehtes lapha exi,lh Tytr)eicea rt tcuesrrut = umepltli anoesdycr ttcreurssu ingnitetrca rgtheoet (ltpimlue bate apteled sheset ksdtcea no tpo of ecah eh,rto raecur ret)aQnty ecsuttrur = niprote trrcusetu ferdmo omrf nfgildo fo all erityrat ustctrerus ot kaem ibingnd tie,ss t.ce
iecnS hte analien aws utp in laepc of het lyiceG,n the irmpyra suurtcetr asw anuble to ormf an plaha xeilh ecsni aalhp xelih sueurttsrc ende a racruailpt ceneeusq g(yl - x- y) in edrro to omrf hognrdey onsbd ot keep teh xileh t.aeslb
tawh is llcaneog ? a aenycdros eiportn rttr.suuec
hewn ouy rmvoee n,lgeyic teh mots datnbanu imnoa idac , mofr hte ecpurrosr celoulem lwil yuo gte a opperr neodsyacr rutuetcsr ? NO
Gly si ,lpoar alienAn is prnnloao adn oh.dihbocypr nssesieM ntnacseenrovoiv ta.miotnu Teseh AAs vaeh feftndier elmcahci poeersrpti hwich lead to diesrtupd perotni indolfg csdn(eroya r)tseuct.ur limaiSr ot Glu - aVl tibinutstsou ni liSeck llCe eei.assD
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$279$49I nkthi it has eiosthgnm ot od iwht engcliy (ude ot sti lslma siez ti nca fit ni nmya lepsac erwhe thore iaomn cidas can tno nda enhce it dvopiser “rurtlstauc esmcs”ocapnt ot het ,ocagelnl .ie. tup a nkik in eth lpaah x.heli) If gnlyiec si delsapcmi by eointgsmh s,eel I ’dtno ktnih ec-laolnorpg can ormf tsi croctre doenrycas s.urttcuer
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