I ufdr,ieg gen--yiXlYc si ylhctnaceli sencoerddi a ra“yipmr iamno dica ucturetsr fo a optnr”ei ceins hte nienditfoi fo a ariPmry uetctusrr fo a teorpin si “a niaelr hnaic of miona cdias”. fI uyo ssem twhi eth rrPayim ru,rtsucet as in teh neqtusio s,met yuo anctno rmfo hte yreoadSnc utctreurs fo hte ,opirtne hcwih is mirneeeddt by eht inoydnggdnebr-oh hhciw orcucs eweentb eth editepp beocbank, teenpndiden fo teh R .orsupg I pheo siht eadm sns.ee
Frmo akweipdii: rcoSy“eadn rttcesruu is afmlrlyo ifedden by eth ptetran fo gehryodn nbosd netebew eht niaom hrygnode dan yrabxocl enyxgo taosm ni het dipeetp koebbcna”. (isheapms ie)mn
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.
ok ygsu nda i uqtoe mfor m0ra:p/adptrccb/.ssmrtiopsilletseefe/si/whw.oehuo2eew1ot4ts/igt-tocn
9"0% veha an fleinbiaited tieecgn unmittoa OLC
11A dan OLC 21A
eucass
ronmlaab onaegllc sirnsi-cngkol via a ylcengi bnotistustiu in het nropgoacell euoecmll "
ihwhc esnma htat OI sha a eiylngc ssobiuttintu dna rrfheeot ist eubanl to fomr a orynsaedc tecus.turru
eDu ot cel'nigys asmll eis,z it scaeter "iksnk" ni the inoam aicd eq.eunesc esheT skkni era edened ot lyocrtcer rmfo the recnyoasd ucrsetu.tr
treOh erans:ws
X--lYyG is bkbcaneo ofr aeclolng lhaap ihacn. 3 alngecol hplaa sainhc plsari ot rfmo epirlt xhi.el ilencyG hsa on R ,ogrup nwoglail ofr exitliflbyi dan fotornaim of ietlpr .hliex No neigylc etpsrenv tish nooticnuus i,siplganr eivetpgrnn eht manitroof fo coalnlge narysdeco s.cuutertr
ecllRa atht lails-hhcaepe adn ebast-sheet ear paxemlse of redaosync s.crttueusr ihTs nac eb ohguhtt fo a niaeastntmoif fo eth laaph h.xeil
NhtAero yaw ot teg at it is aiv lmn:iteaioin
A. gordyehn bdginno tnldouw lalrey ghecan ensci teinreh lainaen nro ygleicn era roa B.pl Gyl &t;g aAl sduth'nlo haengc how peirnlo si ieioddmf (I neam it ,LUCDO fi hreet was a erscit eindcnrha or o,snhmgiet btu nto a getra srawe )nD. iotgnnh to ticeidan ahtt gollance gtdneoderai is tredael ni seperosn to an AA i.tsubnistout o,lAs in teh ctotnex fo IO ihhw(c si teh eennrtsgip atm)icn,pol we yaaredl know ttha hte ombrpel stodne' vhea hnniatyg to od ihwt dane,dgotrie ermo tihw eth chagne ni fotrictnne/uEru tuc.s tysHnole o'ndt nok.w
H’sree one awy ot psore-aeni-eclostmfi ea“erecsdd bgd-yrndnooeh fi”rmot:ona m’I ton a ibg afn of this niel fo ingroesna, but anclethiylc ianneal as a ised gurpo ahs mreo rgdeyhons* for laptinote ogrdyhen oninbgd nath licengy:
nni:aale HC3—
eyg:ilcn H—
,So ”clite“hlyacn, lneaina dulow treipm oemr ogeryhdn-dnbo afritm,noo hhwci gtmih loalw uyo ot liianetme atht oc.cihe
htaT ia,sd ti mssee tsolam spiimosble ot lure uot ot(uwhti yver elcachnit lgekondwe ro mose evdropdi eampeientxlr )tdaa that teh llysthig errlag iealnna osed ton mpriai dnghroye onbidgn wetnbee onegclal uelsoceml iva teicrs lat(s)aip icenrf.nteere nI srimpel esmtr, csnie lanniae is a,ergrl ouy odwul tinkh ahtt it smut woemsoh reinferet whti teh gooinnhyrd-ngbde thta ccsuro hitw the wd-pltiye egiyncl.
---
ttScryi*l ,gapsekni ts’i otn eth eunbrm of yosehgrdn tub salo teh engtstrh fo eth eioldp ttha iitasecaftl hyeonrgd :ondgnib a gyrdeohn ubond ot a slyntogr nlgeiavereteoct umcollee ekil urnleiof wlil raeapp”“ erom iotispev and, uhs,t odnob-rnyghed more loyngtrs with a byenar enyoxg acpmoedr( hiwt a dnehyrog dencceton ot ban,cro orf lpxmaee).
trFeurh riga:edn
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 be invnrktoigeh ti b,ut H bdno fatrminoo fo aa's kames teh daecnrsoy urutrcset fo het toirnpe l(laconeg ni shit caes.) Teh ylG ot alA itsuisubnott sedo tluesr ni sels H donb itfmoonr,a tbu of ulididvain aas' not neewetb nallgeco ullcosmee t(tha imtgh be rmeo fro yararqunte urrc)eutts
ayimrPr tsuetcurr = imnao dcai nre yduccSqeaeeons cttsuerru = ecsurturt drmeof tiwh a sgneil inamo acid unseqeec (aetb eptldae ,hseet aplha ih,xel )rTtyeetai rc rtceusrut = tmelliup rncaysdoe seuutrtsrc nntgitecira eorthgte iuelplm(t abte teldaep eshtse ecsdakt on tpo of ceah to,ehr ternutar eQ)cray trecrustu = prinote urtsucert moredf from nigldfo of lal eryatrit rettscrsuu to maek bgndnii stesi, .cte
eincS hte eaninal saw tup in leacp fo eht lnGeic,y het aiprrmy rstceruut was ubneal ot mrfo na alaph eihlx esnci lahpa ixleh susertutrc eden a ruclrtpaia sueceneq (lyg - -x y) in dorre ot mfor godhnyer obdsn to kpee the xhile e.lastb
athw si oelngcla ? a caedosyrn niretop .rctrseutu
nweh uyo mveore cileyn,g eht omts atbdunan nimao daic , ofrm het erurcpors llcoeume illw you egt a eorprp yorcadens rrtuetcus ? NO
Gly is ,plroa nAinale si aorpnnlo and pdcyoihhrbo. isnseMes raeeoonntcsvniv naitmuto. ehseT AsA vahe eeifntrfd iechaclm proiertesp hwihc dael ot ddiseuptr epoinrt odlgfni crodeynsa( .ue)turrcst iSmiarl to Glu - lVa niituotssbut ni ickleS eCll eeDisa.s
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