I dur,gefi cYneiXly--g is elclthcniay rdscdeneoi a “rpiyram aiomn dcai rtrtusceu fo a t”poenir nisec het defiionint of a mirayPr ecutrusrt fo a eoitrpn si “a iearnl cinah fo amnoi i”cd.sa fI ouy sesm ithw eth raryPmi ,ucrttrsue as in hte utnsoieq ,tmes uoy tconna mofr het anSyocrde cruttsreu fo eth ,oterpin cihwh si etrdemedni by eht ghroobngnydinde- cwhih osrccu wtebeen eth peeitpd nkeaobbc, eneipendntd of the R pu.grso I hope shti eadm n.ssee
rmFo piiaedkwi: yoe“Sancdr tcuetrrus is llymoafr fedndei yb hte tarnpte fo rdognhey nbods neetebw teh omina eygrhndo nda rclayxob ogyenx mosta in het epietdp eacbnobk.” eha(ssmip n)mei
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 uysg dna i oetqu orfm ia/n.hie/etowh0p/4lttsdtto/rc.aii2swoeslgwotfsu:msrbcepermpo/e1-cest
%"90 vaeh na tfelbeiadiin genitec nutmtaoi
LCO 1A1 dna OLC 12A
ssa
uec aaolmrbn elcolagn lkssgniic-ron vai a iylcgne intsbututois ni the eoarnpgollc omeullce "
hhicw manse htat OI ahs a yilcgne iontstutusbi and fereorth ist anuleb ot fmor a acsnyreod sruc.tueurt
eDu to icey'snlg msall zi,se ti asrecet iknsk"" in teh ainmo cida ene.qescu sheeT nkksi ear ededen ot terocyrcl rmof het rycdaenos .tcurrtues
eOrht wnse:asr
-lXy-YG si bneabokc ofr eagnlolc pahla hi.nca 3 egolnalc hapal sanihc rspila to orfm tperil hel.ix ycelnGi sha no R p,ougr onalglwi orf bfytelixili adn foirmtano of rilpet heli.x No cyelgni rvenptse iths uuncotions lpinagrsi, tneipngrev het aftrooinm of lnaelogc acysedonr s.uurtcter
caelRl atth hphcaaseei-ll nad thebasse-te rae psmlxaee of daensyocr uttsucser.r ihTs acn be htguhot fo a tesoftannimai of eth alaph lei.xh
ohtAeNr awy ot gte ta ti is via ieloinni:atm
.A hnogdrye dgnobin toulwdn lerayl nagehc seicn teihnre nalneai orn lencygi rea lao.Bpr yGl gt&; Aal ndluho'ts egcahn owh orlpnie si idodfemi I( eanm it ,LCUOD fi there aws a streci hcrdnaien or thmeno,isg utb not a ertga wneD) .asr nginoth ot cneaidti htta ecllnoga etddgaioenr is daeertl ni neerossp to na AA isunttbosut.i Also, ni the etcontx fo IO hi(wch si het preinnetgs ),lmatonipc ew adraely wnok ttha the omrbpel d'tenso aevh hatgiynn ot od twhi gitderaoen,d mroe htiw teh eanchg in iurottrsctf /n.uecEun stHlyeno 'otnd kon.w
eer’sH eno way to ati-enpom-ielseofscr ecsdaer“ed -ddboengyorhn i:f”anromot m’I ton a ibg nfa of hits ilne of ar,gosinen btu ctlayilcnhe ialenan sa a sdie grupo ahs eorm nds*yrgeoh rof oielpnatt nhyerdog gnindob naht ngeciyl:
n:anilae 3CH—
y:cnigle —H
,So ,c”letnayclhi“ neanlai wodul rimtep emor dnonbhey-rdog aomnofi,tr hhwci itmhg owall yuo ot linmiaeet atth iec.coh
That ,sdai ti emses amlsot bispsomlie ot eulr uot toihw(ut ervy hnltcaiec eldowgenk or omse ipvdreod iapexermtlen ta)ad htta the yitsghll rgelar eainaln odes not irapmi yoenghrd ndbgoin etnweeb clnlgeoa leleusomc vai sertic )aatisl(p ecenrfir.nete nI splmeri stmr,e cines nilneaa is argler, you woudl ntikh htat ti sutm hooewsm nrtfrieee htiw the ngodbnrhno-igdye tath rcsouc twih eth itlyp-edw ygencli.
---
lcStriyt* ,kaengpsi i’st otn teh urebmn fo edgnhryso tub losa the ntsgerth fo eth liedpo htta tcsiilaatef yrengdoh ig:ndobn a drhnygoe udnob ot a tryognsl trvniaeelgectoe loeulcem elki inuerlfo lilw pear”“ap remo esvipiot ,dan h,uts -hegndbondory oemr lsoytgnr htwi a bareny egyoxn m(redpcoa htiw a rdehgnoy ncetencdo ot b,aorcn rfo x)pemeal.
erurFth eig:darn
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 thmgi be nhiinotekrvg it bu,t H bnod faonmitro of s'aa aksme teh ecsyaodrn trecsrtuu of hte nitpeor e(gclolna ni sthi e.ac)s Teh lyG to alA iutntsiobsut odse seutlr ni elss H donb af,rtomnoi tub of nidviduail s'aa not eeewbtn llnogeca eluselocm tt(ah imght eb eomr ofr yarqaeutnr u)rcrtestu
mrraPiy tsruectru = ioman dica noeyn Ssreeuceqdca utsrrecut = tcresuutr ofermd wtih a senlig inmoa aicd ueqeecns b(tae eptdlae htese, haalp ielhx, eerTiact ryt) utsetcurr = uplmelti csneyorda cstrutrues tnrieatnicg tehotgre (meltpuil baet tpealed eehsst esdatkc on opt fo hace ohre,t ear)trcru ayQnet rstrtcueu = tpernoi usttcruer froedm ormf gfolnid of lal ieyratrt uuscerttrs ot keam nbgdiin si,est etc.
ncSie hte naienla saw upt in eaclp fo teh Gelyi,cn eht apmiryr rtusurtce was enalbu to frmo an ahalp hxiel scnei plaha ehxil rtssruuect eden a urlrptaica ecenuesq l(gy - x- y) in dorre to from doegynrh nbdso ot kpee hte xehli s.tebla
ahwt is claegoln ? a eyadocsnr poetrni eu.rsctrtu
hewn uyo eoermv lcyie,gn het osmt tbunnaad ianom cdai , omfr het souprecrr emlucole lilw uoy tge a porrpe oscnedyar etrsurtuc ? ON
lyG is ,orpal elnaAni si aropnlon nad rc.yhopdbioh seMissne vreoitcsnaneonv mtotu.ani hesTe sAA aveh ednitfefr ehimlcca ioeeprstrp ihchw elad ot tiedsrupd otenpir gfnloid dayoesrcn( )cutseut.rr iailSmr ot ulG - alV tinbtsiousut ni lScike lCel .Daeessi
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$379$49I hnikt ti sah snioehtmg to od ihwt nyclegi (ued to sti slalm seiz ti cna ift in nmay lpceas hwere hoter miano cdias nca ton and enche it provdeis tuc“lartusr ocstcn”apems ot eth leol,ngac ie.. tup a kkin ni teh haalp ihel)x. fI legciny si lemspcadi yb gonsmhite ,sele I ntod’ thkin lor-pgeolanc acn morf tsi crteroc sayceondr e.stuutrcr
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