I ugdferi, --cnXYeilyg si tachynelicl enoserdicd a rarmiy“p aonim acdi rcstruuet fo a oeprn”it ciesn the ifonedtini fo a rmayiPr tctesruur fo a rtneipo si “a lnirae ahicn of nmiao sa”idc. If you ssem hwit hte rPimary rsutcrteu, as in eht eoqtnisu ,estm uoy ntnoca fmro the ryaoScedn urecsutrt fo hte itpro,ne ihwhc is rdedeimten yb het bregn-dghynondio wcihh rcucso nebtwee eht dppetie obknabce, neitenedpnd fo eht R rupo.gs I epoh htis eadm sees.n
morF dekiiawpi: ne“Scadroy tuutcrser is aryfmlol feidedn yb eth erntapt of erdhngyo ondbs wnbteee hte nmaio ndohyerg dna oblxycra eoyxgn osamt ni hte tppidee abkeocnb.” aspihms(e n)mie
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 yugs dan i tequo fmro tef/ceeihuerssscwo.dmpilp/o1/:emtolsw-wtceon2rg0ebttirh/pi4stato./sa
9"0% eahv an idifneibatle enegict mtinutoa LO
C A11 adn LOC 1A2
sce
asu rnaoblma elogcnal ln-nrssgiikoc aiv a yliecng sitsutoutibn ni eht lepcolrgona olecluem "
wchhi eanms htat OI hsa a lgyncie tbsitoutnsui dna otreferh tsi lbenau ot rofm a ceansyrdo euscruturt.
Deu to ycl'ingse lamls szei, ti cetaesr nk""ski in the inamo icad eese.nqcu hesTe kkisn rea eedden to ycocelrrt fmor eth esayncrdo rescr.uttu
trOeh :ewrssan
yYl--XG is bcobeakn fro leaolngc ahpla ac.nih 3 eclnlago hapal ncihas asprli ot morf ietplr .ixleh Giecynl has no R ,roupg lainowgl rfo ibxflitieyl dna mrtoinofa fo rpetli hile.x No gcyneil pstverne sith oosuuintnc psi,nlgair veenrgiptn het fnamitroo of neallocg saydeornc trut.rusce
lecalR htat seplhheila-ac dna ea-htesbtes are esaxlmpe of deoarnysc rsrte.tscuu iThs anc be hguttoh of a mntsnifoaetia fo eht alahp .hielx
orAheNt ywa ot teg ta it si aiv oa:tmnelinii
.A hendrgyo dboginn dulonwt yralle nacheg sicne irhenet niaaenl rno yeilncg era pl.o aBr Gly &;tg Ala nut'slhdo gncaeh woh pioenlr is iidmfdoe I( mnae ti LO,UDC fi eetrh swa a ietcsr enirhcdan ro ,imhotesgn btu tno a tgera De.nr sw)a onngith ot cnideati thta acolnelg girdedaneto is dlereat in sspereon ot na AA bo.iutsutsitn ,soAl ni het totxenc of OI hicw(h si hte tpnireesng ,lpom)ciant we deyaarl knwo ahtt teh emprolb toesdn' eahv athniygn ot od wthi gtdraod,iene rmeo hiwt teh heangc in nt.tnucifrrt/cuu Esoe toyHlnse 'tndo kwon.
res’He eon yaw to ofacto-esnpiim-srele cerade“esd nhdgndy-ooebr atrm”foon:i m’I nto a gbi anf of isht elin of gnirseao,n btu yaelthcnilc analeni as a dsei gupro sah emor sedgohnyr* rfo atoptnlie nrgeyhdo gidnobn ntha neycilg:
lineaan: 3—HC
yelnic:g —H
o,S aycthl,ie“n”cl elanain doluw epmtir more bddhrngo-eony ofrit,omna whihc mhitg lwola you ot meiinaetl tath echoic.
athT ,asid ti mssee atmslo sbiemlpiso to eulr otu otwh(tui ervy cechlinta edgwlnoek or oesm doervidp trelempaienx tda)a hatt hte tlhglsiy relagr aainnle odes otn apirim ognryedh nbdiong weeentb aglelcon ulloemecs iav ricset )pliaat(s reenceenr.itf nI rsielmp tsrm,e nsice elaanin si arl,rge uyo ldwou tihnk taht it mtsu hsmooew efnetrier wthi the eggrondn-obiydhn thta orsucc itwh the idlpe-twy ecignyl.
---
tSyi*ctrl sep,aigkn tis’ ont the mernub of ygdsorhne tbu lsao het sethgnrt of hte ieopld atth itsficaaetl yegrohnd bogidnn: a ryhenogd dobnu ot a lygrsont iaevegecnteoltr euecollm lkei urliefon lwli p”pr“aea remo poitevsi and, su,th doobernydhg-n oemr nrgyotsl hwit a nybare genxoy corde(apm hiwt a ydrohgen cdnneotce to rn,baoc fro me)lepa.x
hFteurr eg:ianrd
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 itghm eb ekirnothignv ti ,but H nbod omtfinora of a'sa kemas het asorynced srtutecru of eth nteipro (ncealgol ni this .c)ase The yGl ot Ala ttsbsoituinu seod ltrsue ni lsse H obnd ,oimrnotaf utb of dlniiidauv as'a nto wneeteb algenlco oelslemuc t(hat mgtih be mreo orf ayuaretnrq rcs)etruut
myriaPr cuerstutr = nioam iacd yqodeenra encSsceu tsecruurt = ucserurtt foderm ihwt a esnigl oianm icad ceqnuees eab(t eldptea eet,hs haapl ehxil, ) tycraierteT uuesrrtct = imuetpll ndcayesor escrutusrt ianinrcgtet ttgrehoe u(lptleim teab lpaetde seesht dcseakt on otp fo haec ,htreo rcye nrQu)ttarea eurutrstc = ntporei uutrsectr rmodfe fomr nflgdoi of lla aetriyrt rtucstruse to amek bdnnigi ist,se tec.
ieSnc hte aiaenln saw upt ni eaclp of hte c,Gienyl the airprym trteucrsu saw nluaeb to rmof na pahla lxehi csnei phala eihxl teuscurrst eend a araciutlrp enqeucse ly(g - -x )y in drero to mrof rohengyd sonbd ot ekep eht exihl b.laets
hwta si gocaleln ? a sednryoac etiorpn cuertu.trs
ewhn you remevo lycengi, the mots tudabann mnioa aidc , from teh errpuocsr mloeeclu iwll uoy gte a erropp rdynceosa sructtreu ? ON
Gly is ,apolr linenAa si rnnolopa nad oiyocrbp.dhh nsMisees vorivetscnenona ouittm.na eeThs AAs vahe etedfrfni cachimel rptseirpoe chhwi aeld to ruitpsedd tirenop flndgoi (denyscaor t)tsuc.rrue imrSali ot lGu - laV uotustnsibti in cielkS eCll Disaes.e
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$279$49I nhkti it sah gosmntieh ot do thiw ngciyle d(eu ot ist small seiz ti can tif in mnya eslcpa eerhw etroh amoin cisad cna not and heenc it vpesroid ulttrrucsa“ nspsa”otccme ot the ollcn,aeg ..ei ptu a iknk in the hlaap )heilx. fI ygcinel is piadcmsel by nsigtmohe ,esle I dtno’ hntik -lnagcploero nac fomr ist cerotcr scaodeyrn setuctrur.
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