I gefri,du -gn-iYylXce si ctnicyahell enrdosedic a riy“mrpa aiomn iacd ercttsuru of a ir”tpeno encsi eht fnetnioidi of a airyPrm rstucreut of a rnpotei si a“ aeirln cainh of noima sid”c.a fI you mess hiwt the raiPyrm rtutceus,r sa ni hte qsotieun me,st you tcaonn mrfo the acdyeronS rttuerucs fo teh e,opnrti wcihh is ededtermni yb the nrhybdeg-nndogio chhiw cosrcu ntebwee hte epetdpi oanekbbc, etnnipddene fo eht R rugsp.o I peoh isth maed n.eses
romF kipiwadie: dcreSyao“n urturscet si afylomrl fedneid yb hte patnetr of rhdyogen nbods eeewnbt eth niamo ghdreyon nad lxycoarb oxyegn otmas in the peditep bbnoecka.” isem(saph iem)n
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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wihch nasme that OI ash a igynelc tnibiottussu adn otefhrre sit ublean ot rofm a snredyaco eusrtru.tuc
eDu ot gnslc'eiy mlsla isez, ti ertecas skik"n" ni teh onima idac ceqnseeu. esheT ikskn era ededne ot clotrcrey fmro eth sanerdocy eustrut.rc
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cRaell ttha -haehslaiclpe adn t-saheteebs era esxepalm of csaneryod r.rtstscueu ishT cna be houtthg fo a nmsefaoiniatt of het halpa eh.lxi
NorethA yaw to etg at ti is iav iinonmal:tie
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e’erHs one ywa ot e-cmlpt-isoefiresaon eedrcad“se hnengr-yooddb nat:m”oorif mI’ otn a big fna of sith leni fo ,noersnagi tub ienlhylccta aenailn as a dise urgpo ahs oerm n*grhsdeyo fro aeilotnpt hodengry gbiondn hnta lyingce:
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,oS li”eccayhln,“t iannael wdoul ritemp mreo ohdnneyrdg-ob irft,nomoa cihhw itmgh olwla oyu to tialenmei atht oi.cehc
ahtT adsi, it esesm mltaos ilimboesps to eurl out u(wttiho evry tinclceah negkeowld ro soem pddiervo aprneexletmi ata)d thta teh sytllgih gaerlr innleaa oesd tno prmiia roghndye odninbg betwnee glaelcno oemclleus vai eictsr pai)(tsal eterrfeicnne. nI impselr ,smert cseni linaean is ,aerrlg yuo olduw knhti ttah ti tsmu hemoosw frenrteie wtih teh r-bgoyenninohgdd ttah sccoru whti the eyltd-wip eigylnc.
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rytt*cliS isnpgkea, ti’s ont hte bernmu fo gnsohdrey but losa eht tnsrhgte of eht lepido atht taacifsitle ndeyghor bnndg:io a noeyhrdg unobd to a ogstnrly teeeoacgrtevnli ulecmeol liek lnrfioue llwi paarep”“ mreo epvitsoi ,nad thus, hbygedoodnr-n omre ylsnogrt ihwt a byeran yneoxg pco(emadr ihwt a gnrhydoe cdoencnet ot orc,ban rof )lemp.xea
Frhtuer rngaed:i
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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ncSei teh aienlan aws ptu in pcela fo teh ,cGelyin teh iyarrmp rettscuur aws neubla to ofrm na pahal hxlie ecins lahpa iehxl ctsserrutu deen a alcaurptir cquesene lg(y - x- )y in edrro ot omfr ohgndrye odnsb ot ekpe the helxi et.slab
ahtw is nlegocla ? a srycoedna ipenrto uerrtust.c
wehn yuo emorev ncylegi, eth mots dbuntana manio adic , rfom teh reourpscr luelmoce lwli yuo teg a rropep sayoencrd strceuurt ? NO
lGy is prlao, eiAnanl is opolnnra nad b.cpodrhiyho insMeses veancoinrvesotn anoiut.tm eeshT AAs haev eetifdnfr ehcilmca speporeitr cihwh lead to dtisdepru eoitpnr nofdgli nyac(oedrs curt.s)urte laiSrim ot ulG - Vla sttuutbiinso ni lkeicS llCe Dae.seis
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$279$49I tknhi it has hstmigeno to do htwi yiegnlc due( to tis lmsla izse it nca tif ni anmy leacsp ewehr hteor mnaio csiad acn not adn nhece it sidveorp a“suucttlrr cpacos”nemts to eth lno,lecga e..i put a kikn in hte phala ie.l)hx fI gylcien si mdspcliea by ogseimnht ,else I tdn’o nhkti ac-gopnlrelo acn fmro sti tercocr rnedsocya uctr.sreut
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