I irfegd,u nXic-el-ygY is clatnlyihce sieonrcdde a pmryir“a oanmi cdia teusrcurt of a prneoi”t iecsn the nifditoeni fo a riyrmaP truteursc fo a iprnoet si a“ lrneia cahni of amoin dsi.a”c fI uoy ssem wiht teh yirmPra ,ertusturc sa in het qsitnuoe sm,et oyu noctan rfom eth rSoydcnae rtuusecrt fo het pie,ront whihc si nededrtime yb the bohgg-ennioyddrn whhic crosuc tnebwee eth eippted bkbcneoa, tnidenedepn of the R upo.rgs I oeph ihst amed snsee.
ormF wipikdeia: ydcaeor“Sn erusrtcut si faomyllr deinfde by hte aretptn fo hyrnegod bonds eeebwtn the nomia nyorgdhe and lacxoyrb gnexyo staom ni het eptedip kecboabn”. meiahsps( )enmi
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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cihhw esnma taht OI has a ilcgyen ttsitoniuubs dan hfroteer ist neulba ot rofm a sndeycora ucrustutr.e
uDe ot 'yncglsie lamls i,sez it ectreas kk"nsi" ni eht moian dcia .seeqecnu eeThs knisk ear enedde to etorcycrl rmfo eht nyroeascd cte.usurrt
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othArNe wya ot teg at ti si iva ii:leotinman
A. erhgydon gdonbni tondluw alryel hecgan senic itnheer anlneai onr cigynel rea rpal .oB Gyl ;> Aal dnot'ushl cgnahe owh lpienro si ifiemdod (I anme ti ULOC,D if etehr saw a risetc ndcnrheai or msieognh,t utb ont a aetrg aD w.rn)se thgnion to tneaiidc hatt enclalgo aedgeoirdtn is aeldert ni oeenpssr to na AA tsiist.ounutb ,sloA ni het etntoxc fo IO wc(ihh is eth snrepeting il)omn,tpac we ryedlaa wkon htta teh lmreobp sneot'd hvea hniynatg ot do twhi deetgnadoi,r meor ihtw eht hecnga in ur/Esnteftu cnc.utroi eynHotls d'ton .knwo
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,So n“,hyialecl”tc neanila wlodu mirept moer dndn-yhoebrgo ,iotmoranf iwchh imhgt woall uoy ot maleetiin tath ceic.oh
htaT ds,ai it sesme saltmo imsspeolbi to lrue tuo uht(itow yrve atclnheic wgnelkode ro soem odervipd nipxtemleear dt)aa atth the lygilsth erarlg ainalne does otn aiprmi rdnogyeh dgbnoin tenwebe aelongcl ecslemoul iav strcie tspai)l(a eertenr.nfeci In lsriemp trsme, ecnis eaiannl is ,erlagr oyu ludwo ntihk hatt ti smut ohswmoe rrfnetiee iwth het grnyhnieboodgnd- atht rusocc twih eth tidey-wlp ncligey.
---
tcS*yrtil g,ekpnasi it’s not eth numerb of endhoysrg but osla hte ttgenrsh fo eht peiodl hatt ilsefitcaat grhneydo g:bidonn a ghdreyno doubn to a ntlyrosg liageenertvcote ceoluelm ekil fenriulo lwil aep“apr” moer positevi d,na ,shut ohdynoegbdrn- omre lgoyntrs hiwt a ryenba ongexy r(pcmeoad wtih a rdonyghe noncdctee ot an,obcr rfo eem.)laxp
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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 gmthi be ovienghrtnki it ,tbu H nbdo taofnmoir fo 'asa kmeas het edsoranyc rsutreutc of eth irepotn a(cgellno in ihst .case) eTh Gly ot lAa ntuibiottuss sdoe utlrse ni ssel H dobn fto,ionram tbu of liavudidni aa's tno ewebent gecnolal eomclslue ha(tt mhgit eb oemr rfo uearyanrtq rs)trutuce
yrPmari treucrtus = naoim aicd sa ucycnoeenreSdeq rrctteuus = sucrtuter demrof thiw a nisleg onmai cida enqcseue bt(ae aeeptld te,she alhpa hixl,e ry )trieTaetc etutucrrs = ellmtpiu dcneasyro tctsruersu gtincternai ethertgo (imultple ateb pdleaet eshset acsedkt no opt of hcea ,hoert yucnaratQt)rr ee eurtrutsc = oiepntr turtescur morfed rofm iodglfn of lla ttriraye etuutsrrcs ot meak igbndni ets,si cte.
iScen the aanelin aws upt ni lpcae of eth ilyn,cGe eht impyrar crtruteus was aunebl ot rfom na phala lxhei esicn ahpal lxihe sutustcrer ndee a ictrrapalu euesncqe (lyg - x- y) in dreor ot mofr hgyeondr sondb to ekpe het lheix atlse.b
hwta is geanlolc ? a ecynoasrd rnpoiet stceuurt.r
whne you remoev cngiye,l hte tsom nbdtnaau aoimn idac , fomr het rreopcsur eoumclle llwi oyu teg a rpeopr nesdacyro crteuurst ? NO
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$279$49I khint it ash enthgosim ot od ihtw iyenlgc e(ud ot sit amlsl esiz ti can ift in myan csealp ewehr thero aonim caids can not dna ceehn ti oidvsepr rsur“tatulc ”ptsnosceacm to teh lna,goelc i..e utp a iknk in hte alahp .ilhxe) If ngeclyi si decmispal by nghmsotei e,sel I tno’d ihntk -aolclerngpo nac rfmo sit ctcrreo sconadyer rturectu.s
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