I drue,fig lgyc--YeXin si cenyitcllah oiecsedndr a rir“ypma namoi icad curtutrse fo a prtneo”i ciesn eth inindoetfi of a aiyPrmr uctrutres of a pnriteo si “a ealinr ihanc fo noima said.c” If uoy msse ihwt eht rrmyPai rucerustt, sa ni het sqteoiun em,st yuo tncaon mrfo hte ecrdonyaS utercsrut of hte oi,ertnp cwhhi si mdendteier by eth hidyorgeo-nngdbn hhicw orscuc bweteen teh peitdep cnobbeka, inedpnedten of eht R rpos.ug I ehpo shit amed s.enes
Frmo aewiidpik: d“Soceyran utescrurt si rflalymo nfeided by eth npattre fo ogrnyedh dbsno tewneeb eth imnao rgdhoeny nad oylcbxar ogyenx masto in teh eiptped aeobnkcb”. epsimhas( m)nei
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 usyg and i qoute fmro i0b.isetr/pultsc/s/do2i:osec-ht/thowsw.tfirlmarpsnamo4w1peeee/etotgc
"%09 vhae an enltiieadfbi tngciee untmaiot OL
C A11 dan OLC A12
sausec
mraoanlb nllaceog sngrlin-ikosc aiv a ilcynge tssituiubtno in hte pellcagnoro cmoeleul "
iwchh asnme htat IO has a yncelgi utnisitbostu dan eorhterf sit ualben ot orfm a csorndyae tutrsue.cru
ueD to 'sengycil amsll zise, it eacrtse sn"k"ki in het anmio adic cns.eqeue ehTes snkik rea ednede to ryortclce fomr het drnsaecoy eruursc.tt
tOrhe s:rwnase
lG-y-YX is ebbkcnoa fro onllacge aphal ni.ach 3 cognlale aahpl anhsic lsraip to fomr petirl e.xilh lceGniy ash no R rp,guo lgnoiwal orf eltliyixbfi nda motonrfai of tirlpe x.lihe No cgnliey nsprevet ihts unstuocnio ,niglipsra ngprveeint het ntioorafm of ecaolgln eraoncsyd .trctsrueu
eaRlcl ttha slaeahcp-lehi dan haet-tessbe aer exaplesm fo dorsanyce tursr.utecs Tihs can be uthotgh fo a snnfteitaimoa of hte lhapa .hlxie
ertNhoA ayw to etg at it si avi ininaoetm:li
.A hgeorydn nnbdgio olwdutn ayellr caeghn cisen heirent aeinnla rno ciyengl rea .Bpola r lyG &;tg lAa n'slotudh nehcag how lnrepoi is ddfiimoe (I nmae ti U,CLDO fi htere aws a seritc caidnerhn ro ohigmnst,e btu tno a ertag w Dnse).ra gnonthi to ntiecida ttah genclola redeodtgnai si taeerld in neopress to an AA ssottn.ubutii Aso,l ni teh ttxcoen fo IO hcw(hi si hte npertinegs ntm)ocilpa, ew leyadra wonk ttha hte epmlorb sndeto' aehv ntigyhna ot od wtih iertdoegdan, emro with eht agcneh in .uoE /enrustticfcuntr lHsteyno 'ntdo .oknw
eeHs’r oen ayw ot ectriealmnoifoe-s-sp rsadceede“ gndn-borhedyo ftaoo:”nimr I’m nto a gbi fna of ihts ilne of ,srngeoain tbu ylcithanelc linanae as a eids ogpru has omer *ysdrgnohe rof eptiolnta oderhyng bondgni naht enyligc:
aanel:in —3CH
ye:gclin —H
o,S eatl,lcin“h”yc niaaeln wdulo mipret erom noenb-odrdyhg noimtaof,r hihwc hgtmi lwlao yuo to melieanti ahtt coehic.
tTah a,dsi it essem tmolas isbopismle ot uelr out iwhoutt( eryv icalehtcn eodwlgnke ro oesm rdvipoed extaprleenim dt)aa atht het lhgstlyi elarrg nleiana odes otn aipmir nedroyhg dnnibog etebnew anellgco lomceusle aiv siterc ata(lp)si tniefrrcne.ee In rslipem mt,sre esnci naniale si l,egarr you wdulo ntikh ahtt it tsum womohes eernteirf htiw het gndriogen-nhybod ttah ccours tiwh het -dyiwpelt ilyceng.
---
yrlitt*Sc ,spekaign ’tsi nto the erbumn of sdryengho tub oasl the tstrngeh of eht odlpei ahtt fstiailtaec gyhroend odingnb: a nregoydh uondb to a slonygrt roetvecgleienta loeuclme kiel nfeluroi wlli apea“r”p erom ipsvteoi nad, hs,ut odb-nnderohgy roem grsolytn ithw a ayerbn yxgone ocdamrep( tihw a reoghdny ecctnonde ot ocbnr,a rfo a.eelp)mx
rtreFuh egir:adn
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 hgtim be rvningihteok ti bt,u H bnod oaortfimn of asa' mkaes the odsaecnry ruteurcts fo het toprein olaeng(lc in tshi s)ca.e Teh ylG to Ala itttsuonsbui osde tlresu in ssle H obnd tom,nrofia utb of lvadnduiii as'a otn twenebe gconlael sleolmeuc (hatt gthmi be rmeo ofr quytearran truesrctu)
raPriym crsuttreu = onmai adic dSueaco eysrecnnqe ttrursuce = rrusuetct romfed wiht a nilgse oinma ciad eucensqe ateb( delpeta h,stee apahl e,ilhx ceT etta)rriy ucterustr = ieltmplu nceayrods escutrsrtu raitntinegc hrettgeo pm(ueiltl baet eapltde sheest dcaktse on tpo fo ecah ,eotrh )n reyetaQrutcar usutrerct = orpniet trtesurcu dmfroe ofmr nilfodg fo lla raeryitt rrtsucesut to akem gnbidin eist,s e.ct
ecSni teh aanneil saw tpu in palce fo hte clGy,nei eth rapimyr setcrtruu aws labenu ot orfm an hlapa xileh sienc lapah lheix ttucrsesur nede a rtiraaulpc enusceeq lyg( - x- )y ni order to fmro grodynhe dnosb to eekp het xiehl lat.ebs
hawt is nalcogel ? a sndryoace eiptnor ercturus.t
nweh uyo vreeom ieglync, eht tosm nnuaatdb onami dcia , rfom eth cuoprersr eoelmulc liwl ouy teg a oeprpr cysoaernd trutuscer ? NO
ylG si aorl,p nleinaA si lrooannp dan o.dphhcrbioy siseesMn varvciootnseenn tti.nomau eehTs AAs heva tenerfidf cmilaceh prsretoeip hhciw dlae to trddipseu petnior ofglnid ocnyrads(e sc)er.tutru iirmalS to uGl - lVa tubitiosunst in Slecki Clle saDie.se
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$279$49I nitkh ti has nesthiomg ot do whti icngyle d(eu ot tis msall size it nac tif in mnya palsce rehwe ohter mnoai dcisa anc tno and cnehe it ripsedvo ctslurt“rua etsac”osmpcn to teh na,llgcoe .ie. tpu a nikk ni het palha ehxi.)l fI lencgiy si paidcslme by ihgsemton see,l I tdno’ itnhk rnoel-agolpc nca morf sti rtceocr aosryednc uetrt.cusr
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