I gefidru, c-g-iXnelYy is nehtcliylca dnecsrdeio a mp“yrira iamno dica recsturut of a toeinrp” sncie eth nfeitoidni of a rriaPmy rrctueust fo a etonipr is a“ rielan chnia fo aomni d”s.ica fI yuo smes ihwt hte Praymri tcurret,us sa ni teh eosntuqi tes,m uyo ntocan rfmo teh erdyaSnco ttcsrueru of teh epino,tr hchiw is rtidnemeed yb het oh-ggindbdnyreon cwihh coscur neewebt hte idepept enockbab, eedpdnetnin of het R osrg.up I ohep itsh amde ness.e
Fmor ieiwkdapi: noe“Sdyarc urtcrutse is amylolfr eeniddf yb hte etaptrn fo enhyodrg obnsd neetbwe the ainom honryedg dna aorlycxb onyxge sotma in eth ptpeied ncabbeko”. sa(ipsehm mni)e
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 uygs nad i eouqt rofm lsfocperriitesotgwr1a:tuabdtps0e/o/thste/e-4whec2o.io.pt/ms/wecnmsli
90"% veha an iebenfdiatli iectegn tonmitau C
OL 1A1 dna COL A21
auses
c rmbnaaol lcgeolna sgrosi-ciknnl aiv a ieglnyc btsuittsinou ni eth pcgeolornal cmleluoe "
hwhci senma that OI ash a gliyenc tnsoutbsiuti adn teehorrf tsi ealubn ot rmfo a sdenoaryc ut.reuurstc
euD to egisyn'cl lmlas zeis, it cearset n"is"kk ni eht oniam caid ecueesnq. eThse skink are deedne to coyrectrl ofrm teh reocnysad screruu.tt
rheOt sen:raws
-lyXY-G is ckabbone orf caengoll paahl ac.inh 3 llgaocne lpaah hanisc aprils to ofmr tlriep l.hexi ceiGnly ash no R gpru,o gloliwan for ieflilbixty adn rmoitfnao fo ietrpl el.xhi oN geclyin esrntepv tihs otcnsiuuon ili,spagrn ginrvnpeet teh ntiarfmoo fo egoclanl aocsredny ettucrrs.u
lceaRl ttha eacsllihpeh-a dna sstteha-eeb aer plaxseem of sarnyoedc urtsrtuec.s siTh cna be ththguo of a otimfninestaa of the laahp e.hixl
AtNroeh ayw ot gte ta ti si via inamiil:nteo
.A negrohdy nbidong lnduwto llraye ncaegh iecsn eientrh innlaea rno gyenicl aer l ap.orB Gyl g&t; Aal otsnhudl' ehnacg who iolenpr is ddmoeifi I( mane ti CODL,U fi there wsa a tscire ahrndcine or mon,iegths ubt not a trage a)e r.nsDw itongnh ot tiidenca ttah leaocgnl artneigeodd si eledart in rpeneoss ot na AA nstoutiusib.t Alos, in het ttecnxo fo IO h(hciw si hte nrpengiset i,npltacm)o we aaryled owkn taht eth boemrpl sdt'eno haev tignanyh ot od tiwh ,negrodeidat moer wthi teh hecagn in coreinu Ettt/funcsu.r lnesHtoy dnto' .wkno
es’rHe eno awy ot ceforsoaee-i-iptlsmn ereaedsdc“ brdeohdonnyg- n”fit:mraoo ’mI ton a gbi fna of itsh ieln fo aonni,rseg btu litycenaclh naaniel as a deis pourg sha ermo rgesdhyon* rfo opttenlai rngdehyo nbiognd athn ygcelni:
nnial:ae 3H—C
nelcg:iy H—
So, hceya“clntli”, nilneaa dlwuo pretim mero -dodybehorgnn in,rfomtoa cwhih mgith alwol you to tmiileena that cie.hoc
Ttha da,si ti eemss smotla ibsplemios to rlue tou whutoit( evyr cchailnet owednkgle or mose poddervi aeteprmienxl a)atd ttah het tyglihsl ragerl aainlen dseo nto mipiar rodhyneg nbdingo tneebwe caelngol ulloecmes avi ersitc aips)lat( ectfrrninee.e In rmsipel sr,mte ensci nlaeain is rg,arle you wduol itnkh that it smtu osmeowh erinertef twhi eht yghonennodd-grib atht urcosc ihwt eth dplyw-tei cenylig.
---
*tryltciS ai,gksnpe tsi’ tno eth brumne fo doneghrsy ubt asol teh erhsnttg fo eth eioldp taht feaclaitist eohdyngr on:bdgin a nhyogdre donbu to a nolgsytr toegeenravcetli luceolme ilek ulinfreo wlli ”rpeaa“p rmeo iespovti and, ,htus ybo-nedrodghn reom gornsylt hiwt a yeabnr enyogx pam(ordec whit a rgeyndoh eotncecnd to arbcno, rof ep).xelam
turrheF rangid:e
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 timgh be kvihegionrtn ti b,ut H bnod mofranito of sa'a kasme eht sdaeynorc ctrseuutr fo eht rnoteip oegal(nlc in stih ea)sc. hTe lGy ot aAl tutbiotsunsi oesd usetrl in ssel H ndob aomtfnoir, tbu fo andividlui a'sa nto eeetbnw clneloag clseoeuml t(hta tgimh be remo rof rataqyruen rsuutrec)t
mrrayiP usurtcert = naoim cadi eedo reSseanyccunq seuuttrrc = rreucutts edfomr tiwh a lnegsi moain daic nesucqee a(etb dapeetl ,tehes lhaap elhx,i ctit)Trre aye urcturtes = elupitml drayoscen tusutcrers atcitigernn teeorhgt eutlm(lip abte apetdle tshese etdkcsa no opt of aehc roteh, r trnaacreQyetu) tsucterur = trnioep erutrutsc odrfme fmor fogdinl fo lal ityaetrr rusucttres ot meka nidgbin isse,t e.ct
Sniec het naaelin saw ptu in leacp fo hte ln,cyeiG the mpariry ctrstuuer asw elnuba ot mofr an aaphl elhix nseci aaphl ielhx utscstuerr dnee a pitlaurcra euseencq ylg( - x- y) in roedr to ofmr gneyhdro bodsn to epke het ixhle bets.la
what si naeollgc ? a cydnroesa einrtop trtsucer.u
ewnh oyu vemoer ,gnilecy teh tosm anndtabu nomai diac , romf eth poucrrrse eelmculo lwil yuo etg a eppror dsoyarecn rtuecrtsu ? NO
ylG si lor,ap iaAlnne is opnornal dna yrh.oihcopdb Meinsess oravtcnsoeivnen tntiumoa. esThe AsA aveh dfrneefti hclmaeic sproiteepr hicwh dlae to tdreipsud poinert gdnfoil ensdoayc(r cu.uttrre)s lrimaSi ot Gul - alV binstttsuoui in Selcik ellC iDess.ea
submitted by ∗wasabilateral(47)
It can be re-accessed by making a purchase.
Purchase your membership here
$279$49I inthk ti sah mhiengsto ot od with elcynig (edu to ist slmla esiz it nca fit in nyma lpsaec rhwee eothr omnia iascd cna tno dan ehenc it vsoepidr tulrrstau“c tosnepams”cc to the gecoanll, .ie. put a knki ni het hlpaa l.)hixe If eygcnli si maeislpdc yb oisetghmn e,sle I on’dt khint lecg-ralpono cna ofrm tsi orrtcec aondsryec streuutrc.
$279$49