I igeud,rf yi-e-YgclnX si hatncllieyc drsinocdee a y“rprami oamin acdi rctuesutr fo a tirnpeo” since teh idtfnoiien fo a aiyPrmr ecsuurtrt fo a etnprio si a“ lrenai cnhia fo imona c”.dasi If yuo essm wthi teh iPyrrma uer,cuttrs as in het ouistqne m,tes oyu ntonac rfmo eht oaycnerSd uesttrurc fo eth eoip,tnr hwchi is eeddnertim by the iohbdnr-ggnyeond hwcih orcsuc tebneew teh ptepdei obceanbk, tieeddnnepn fo eht R .osgrpu I eohp htsi eamd nse.se
Fmro iwpaeikid: ynScodare“ reutrtcus si rafymllo difdnee yb hte aettprn of eodgnrhy nobds tnbweee hte oniam donyehgr adn axyrlocb xngeoy ostma in eht pdetpie baoncbek”. (maieshps i)nme
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.
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whchi nmsea ttha IO sah a gncyeli oiitsnuttsub dan fereothr tsi lbenua ot rmfo a adncrsyoe rc.seuutrut
eDu to eclynisg' aslml ,isze it escaret sk""ikn ni eht ioanm cdai qeen.cseu eesTh kkisn era nedeed to ryrletcoc from eth arydescon urtstce.ru
eOtrh erasn:ws
y-Gl-YX is okbenabc orf agclleno phala .niahc 3 egoclnal plhaa scniah lisarp ot romf irtpel i.lexh cnlyeGi ahs no R orgu,p liglnowa for yteliiiflbx and namrtoofi fo ilerpt heil.x No eliygcn nprstvee tshi ucooisnnut agpri,lsin gnvreetnip hte iatnmfoor of nglaolce cyroaensd ctue.ursrt
alceRl atht capls-ihlehea nad stthbae-ees aer apleexsm of yaedsornc ttusr.rsuce isTh nca be tgohhtu fo a imnatsoiaetfn of het apahl ih.exl
eANthor yaw ot teg ta ti is iav ienl:tiianom
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’serHe noe wya to aotemer-eilocfns-ips aerceddes“ edondyogrhbn- aitn”orof:m mI’ ton a ibg fna fo tihs niel of i,nnsargeo btu tnchlaeycli lennaia sa a dise orugp sha emor e*nhsgdroy ofr pettnoial nredhgoy dinngbo hnat lignyce:
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,oS y“aitcehcl”nl, aniaenl lowdu ipertm mreo ngronhdyd-boe ntramioof, whhci tghmi lwlao ouy ot tnieiemal ttah hc.oeic
htaT si,ad ti meess oatlsm piiesmoslb to uler out (uitthow yevr ncehlatci dolnkegwe or osme ddrevpio axmentreplie )data atht teh hytsilgl rargle nialean odse tno aiimrp yrondehg onbndig etbwene eanlgloc eoecluslm avi ercits paai)lts( ticnneerefr.e nI mlpires etrm,s iecsn alninae is agl,rre uoy ouwld tinkh that it mtsu ewhooms ifntereer twih teh igbonnoghded-rny atth ruccos ithw eth -wedtyipl gcyenli.
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r*ytlScti snaiegp,k sti’ tno het embunr fo ohegyrnsd tub olas teh tsgenhtr fo teh edpiol ttah ttiecalaifs ngheydor dninob:g a rgnyoehd dbuon ot a ntglrsyo vatrneelgotecei uemlcoel ielk ufnoreli ilwl eparap”“ orme itivsoep ,dan suh,t hdo-gdbernnoy meor ostylgrn iwht a anreyb gnoexy ro(caemdp wiht a gedyhrno cenctdeno ot r,cabno for .eepxma)l
hFrertu dgn:eair
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).
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nciSe hte nelniaa aws ptu ni aelpc fo eht y,iceGln eth parrmiy trsceuurt asw uebanl to orfm na palah xileh inces apahl elihx tcturssure ende a ptralarcui scueqeen yg(l - x- )y ni rrdeo ot frmo negyohdr obdns ot ekep teh hlexi bels.ta
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wenh yuo eromev ,gicyenl teh mots aadnntub imano acdi , omfr het ersrpucor comeelul wlli uoy teg a prpeor yaerdoncs cturretsu ? ON
lyG si olp,ra inaAlen si nnoolpra dna brodohypchi. Msseesin avstrnenicvneoo tm.ntaiou heesT AsA heav ffretnide emcliach eertpipors ichhw lade ot dtpdurise opernti golifdn odesarcn(y uc)tt.errsu lmSriai to ulG - Val suoutibnttsi in Silcke leCl eaesiD.s
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$279$49I nhikt ti ash nsomtiegh ot od wthi eyicgnl de(u ot tis asllm sezi ti acn itf ni amyn pelsca rweeh roeth omian casid can ton nda cehne it orivedsp ttsrcraulu“ ct”ecspmonsa ot het c,legoanl ..ei tup a nikk in eht hlpaa ihxel). If cneigly si isdmpealc yb smiengoht sle,e I on’dt kntih golancleopr- acn from sti occrrte eysdnroca tteursu.rc
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