I fd,rgieu gely-cYi-Xn is ncycllaieht cdesnriode a ry“ipmar inoam ciad ttusurcre fo a oienrpt” nices hte itiidfneno of a yaiPmrr rucuetsrt of a onptrei is “a ranlei hcnia of miano .adic”s If uoy ssem ihwt eht yrrPmai trt,uusrce as ni teh ntoiqeus emst, uoy ntonca omrf eht erSdyncao eutturrcs of hte oreip,nt chhiw is edretnmeid yb the gd-oorndnbignhey whcih scucor wteeneb hte tdippee bbncaoke, enedndeptin of het R psug.ro I poeh ihts edma eesns.
mFor ikpaeiiwd: neScraoyd“ rctturseu si alrmyofl dndfeei by eht neprtta of enoyhdrg odnbs wbeteen teh monia ornydegh nad bxyraolc egnxoy matos ni teh peitdep kceabbon.” hiamssp(e )niem
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 uysg dan i etqou rmfo i0/forsobe/1.nacleprt2s4pwdseahittthsrs-pwt/eotsio/lg:utmmeci/ceeo.w
"90% heva an efliaitendbi egcneti umanoitt OLC
1A1 nad OCL 2A1
cseusa
noaamlbr ogelancl nig-srklincos vai a lnicgey tnitiuuobtss ni the nrcaoglloep eoemlluc "
hicwh naems atth IO sah a iycegln utonssttbiui and heeofrrt ist baeuln to romf a yoreadncs etusturrc.u
euD to ie'cgylsn malls s,eiz it ecasetr sk"k"in in eth omani dica euese.qnc sTehe knsik ear ddeene to orcreclyt frmo hte cyaenorsd eurrutsct.
hrOte wrss:ena
-GY-ylX si ebkoanbc ofr lcoglane ahpal hiac.n 3 ceolangl alhap snicah apilrs ot form tlripe i.xelh ylnecGi sah no R po,gur oaglnlwi rof xllibiiytef nad ortnfiamo fo ltierp hi.exl No gneyicl repnsvte ihst uctusnioon g,sariplin pertgnvine het otaimornf fo cgaoleln eydrcsnao seuutrtrc.
Rclael tath ehspcaielah-l and tat-sshebee era aeexslmp fo roancedys uturrs.estc iTsh anc be ththogu fo a iosiatnamtefn fo eht ahlpa hlxei.
ehAotNr awy ot etg ta it si iav imelionntai:
A. nrgoyehd odginnb wotuldn yaellr egcnha necsi itenehr aanenil onr lcngeyi rae o Blp.ar Gyl t;g& lAa 'tsuoldhn cngaeh ohw leponri si iidoefdm I( eman ti ULCO,D fi eethr wsa a isrcet nhacnerid or ntsmigheo, tbu tno a garte a )ewnrsD. tghnoni ot citidnea ttha gaeolcln ntedegadior is eertald in senpreso ot na AA i.tstuoustibn Aols, ni eth ncxtoet fo IO hwc(ih si hte niprsnetge pto),icamln we dreyaal onwk htat hte poblrem oedtn's vaeh aihngytn to od thwi nao,deirgted rmoe iwth hte acghne ni trouE.te/ucf rinusctn lyseoHtn dnot' .nokw
seHe’r noe way ot m-efe-esoplsicrtonai rsdeea“cde ddhgoynreb-on fa”irtm:oon m’I tno a gib fan fo isth neli fo gor,einnas but tnhcaclyiel nilaean as a ised gupro hsa meor ngho*dyrse rfo etltnoipa erhoyndg dbgnoin htan gniceyl:
n:nlaeai C—3H
lineygc: H—
S,o il“cecytl,hna” ainelan ouwld etmpir oemr yedb-gnorohdn nfarooit,m hwcih hgitm woall ouy to ieateimnl htta ceohci.
Ttha s,aid it smsee asomlt iiospebsml ot urle otu othiuwt( vrey liceactnh lgewdenok or esom pioderdv etanmlxipree td)aa hatt eth sillhgty arlreg nanaeli osde ont imrpai nehogyrd gdnoibn ebetwen lloencag oecmuelsl iav icsert la(satpi) rrneetienc.ef In lipsrem ,mrets ecsni aanlnei is arl,reg yuo luodw nkthi htta it mtsu moshewo trnfeeire hwti hte hnygoe-brdgodinn ttha ccosru hwit het ie-pwdylt enigcly.
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itSl*rtcy isgp,nkea sti’ tno teh bnrmeu fo oedsrgynh but laso hte rtstnheg fo the eoipdl atth leisfaicatt nrohdgey i:dnngob a rneygdoh doubn to a srgyltno oceatteengeivrl elmuceol ikel lonrfuie wlil rpap“ea” oemr iisvoept n,da hts,u nboedoyhdnr-g mroe ryntogsl htiw a beyran ngyexo p(cedoram htiw a gondrehy etceconnd to ancro,b rfo .elmx)pea
rhruFet :geadrin
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 tgimh eb gohtiniekvnr ti tb,u H dbon rmiftaono fo a'as meask hte oeycadsrn tresruutc fo the erniopt llane(gco in sith esac.) ehT Gyl ot laA usiuttsonbti dseo leustr ni ssel H nobd rnofto,iam tbu of diiudnvial 'asa tno teweneb gcellano scelluome aht(t thmgi eb mreo fro taeauqyrrn )ucsrtture
rmiyaPr ruuttcesr = omani diac ydeec anronqSsueec csrteuutr = cturterus ofmedr thwi a ignesl oianm cdai uecseeqn teb(a deaeplt e,tseh alpha exih,l arcetTet)yir utcruestr = ilmutple eoacrsdny etucssurtr eaicnrttgin gothrete uietplml( teab edletap tesshe edsackt no pto of aehc ,orteh ttrearnQauyr) ec tuuctrres = inoetpr tcuetsurr feromd rmfo idglfno fo lla ryeratti srutscerut to amek gndibni i,tses cte.
enSci het nealina saw upt ni epcla of eht ilenG,cy eth yampirr uurrtetcs aws elnabu ot orfm an laahp iehxl seinc alhpa hexil ecrusutsrt deen a irualtrpca ueenqces lg(y - -x y) in eorrd ot rfom eyrhongd ndbos to eepk the eihxl b.atesl
whta si olgcanel ? a dyacesrno riotepn u.retrtcus
wnhe ouy ovmeer nceyigl, het mots aunatnbd aomin caid , fomr het cesrourpr lleuomec liwl uoy gte a preopr yoanrscde sttrrcuue ? NO
lGy is ar,opl lAnaein si aronnplo adn .obhrcipyhdo essneMsi onivocsvnatneer .numtitoa esheT AsA hvae fnefitdre ceiahmlc eptroeprsi hciwh elda ot pditsrued rtenpio fnidolg sdao(ceyrn tut.)resucr rSmilai ot ulG - laV tibontutissu ni leSkci llCe Da.siees
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