I efu,drgi --yYnlegiXc si lcictaylehn rideoncsed a ripya“mr aionm icad trseuruct fo a eop”irnt ensic the tniinfdioe of a mrarPiy usrtcretu of a otrpien si a“ enirla nicha of oiman .”sdica If oyu mess iwth het rmraiyP ruuc,tters as ni teh snoqtuie em,st oyu tonnca omrf eht rSeyodcna ctstrueru fo hte eprio,nt ihhcw si edteiemrnd by the oydnierndhgnog-b ichwh croscu etbnwee the epidetp kneoabcb, edndentnipe of eth R go.upsr I pohe htis dmae e.sesn
Fomr awkidpeii: “ayrednocS ertcuturs si lomylfra nefdedi yb the entatrp of nrdhegoy ndosb eewtben the ioman ygeohrdn and xcarloyb nxegyo saomt in hte idepetp bbanocek.” ahpsmsie( emin)
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 sguy nda i teoqu from pnsi:e-/otsce.wlpsri.dhstoseapeaeheo/t/cttmbifrir1gol4/cuwwsoe2mt0/t
"09% evah an tfbdieneilai gnteeci tmnuotia LC
O A11 nda CLO 21A
ssauc
e almronab olcnagel snsnricglkoi- iav a ligceny sisotuittbnu ni het cgopellonar ucleolem "
ihhwc smaen htta OI sha a elgciny tustsuonibti nda rfhreteo its enlbua to rfmo a csardnoey ueutrscr.tu
eDu ot 'ngileycs malsl ze,si it ascteer ""nskik ni the inmoa idca eqsceu.en eehsT skikn era eededn ot rrcoelytc frmo het acnrsdyoe cru.ttsreu
hetOr ersw:nas
Y-yXl-G is nebkoacb ofr gelonalc palha hinca. 3 nclelgao pahla snhcai lapsri ot mfor ertipl ehilx. Giynlce sah on R ,ogupr lnlaogiw rof ftiliblyxei nda nofmtraio fo ilrpte i.hexl No yneilcg rsnvtepe this itonuusonc iigsnarlp, gervinetnp hte tnaoroimf fo nlaloegc codsneray rtutuecrs.
ecllRa htta hahlpiacs-lee dna ebtaeshte-s rea emelsxap fo dsoaenrcy srecusu.rtt isTh nca eb uthhotg fo a naisafmeitnot fo het pahal ileh.x
erhotNA wya to teg at ti is iva a:ienoimitnl
.A eodngrhy nidgonb ltwnuod llraye hecnag iecsn iterhen einlana rno nycgeli rea l. orpaB lyG &;tg aAl tdhl'osnu haecgn who prineol si mifoided (I eanm ti COL,UD fi tehre saw a eicrts hdnnicear or is,hoenmgt tbu not a garet sDan. rwe) ohtingn ot icanietd ttha enollcag idetreagndo si raeeltd in ospresne ot na AA tsnbtiusuto.i Alos, in teh tcotnex fo OI whic(h is teh nsteirpnge i)tlcapmno, we edarayl wnok that eht olmprbe etosd'n heva ngyntahi ot od with ,toeidadrnge orem itwh eth hganec in unteEt rccuuosi.ft/rn sleyHont no'td wnok.
’eesHr oen ywa to r--ltseesoeaoiimcnpf cdd“eseare odnrbn-edoghy f:nai”omotr mI’ tno a gbi fan fo itsh lnie of rnise,ngoa tub ctlcylhaien ieanaln sa a dise gourp sah erom *nrdeogshy rfo ttpeonlai hdenrygo ndoginb than cngylie:
enaa:lin 3C—H
:yncglie H—
So, tniy,cla“ehcl” nanilea odlwu pimrte omer neodnhbrygd-o ro,oatfnim hiwhc mthig wlola oyu ot amiteilen ahtt eohc.ic
Thta ads,i ti msees tmsalo oebsslmiip to urel out tth(wuoi ryev itnaccleh wkleogend ro emos ierdopdv meaeteirxnpl d)ata thta hte ghylstli aegrrl nialnae oeds tno mrpiai gdeyonrh niogdnb etweben gnloecal mueleocls iav rtsiec tpsiala)( ernfeieenrtc. nI mpilesr tsmr,e escin nanaeli si arrg,le ouy dlwuo tikhn ahtt ti umts hoowems nrfreeeti ihwt teh hb-norgnnyogeidd htat ccrous hwit het ledti-wpy lgyenic.
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Srttlyc*i epnisagk, ti’s not het reumnb fo ghodnysre btu loas eht sttergnh fo eht idlpeo ahtt leaiatfcsit rhdneoyg :ionndgb a ydngreoh donbu to a tongrlys elttarvcenoegei leucelmo like iofrluen liwl ”aperap“ oemr siiotvpe ,dan sh,ut edy-brohngodn ermo nlgyorts wiht a byaner yegnox pdacmro(e hiwt a yronhegd nencctode ot bacon,r rfo )map.elxe
hurFert nag:rdei
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 mtihg eb ktvghioinenr ti b,tu H ndbo arfnomoti of 'saa aeksm the aocnedsyr euctsrrut fo eht ponrtei gn(claeol ni tihs se).ac eTh lGy ot alA ttiuuiostsnb deso utlres ni less H dnbo ,romnatfio utb of uvaliididn asa' not ebtwnee ngcaloel suleocelm (htat mhitg eb eomr rof unatearrqy ruetcr)stu
irPymar ucrsrtteu = imoan diac sSuoeqcynrde eeanc trurtuecs = tcrsuetur deomfr htwi a nlgeis nomia iacd qunseeec e(tab eaedlpt h,tese lpaha xehl,i treaTi)ecr ty utertcurs = tlpeumil yndcoeasr russetrcut tticnagrnie eergtoht ll(iemupt abte tadelep esehst aedtcsk no otp of hcae htreo, )yQruetreat cnar uecstutrr = pnierto uuetscrrt fmerod romf lfgdnoi fo lal rariytte urtestrcsu ot mkae ninbigd stsie, te.c
Scnei het ainnlea asw utp ni clpea of het icyelG,n teh mprriya cutrtseur asw uneabl to rfom an plaha ielxh secni lphaa leihx scrsureutt ende a apicarlurt nueesecq (gly - x- y) in erord to morf rgnehoyd nsobd ot peek eth ihxle ta.elsb
hatw si legolnca ? a endacyros onrtiep sucetrrt.u
hnwe yuo mvroee eyin,glc the msot anbntdau omani aidc , fmro het cuprrroes umlecleo liwl you tge a eroppr ornsycade ecrtsurut ? NO
lyG si l,raop inelnaA si oronlapn dan ropdby.cihho seesMisn nivveeonsoatcnr iatomnut. Teehs AsA eavh erdffntie ehmclcia seriprpeto hicwh elda ot pdudrties ioertnp ondgilf (rasoncdey esrtuctu.)r ilamiSr ot luG - lVa utbnisuistot in Seiklc Clle .ssaeiDe
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$279$49I nikth ti sha hgneimots ot od hwit icyengl d(eu to tsi lmsal isez ti acn itf ni nyma cseapl rhewe hroet onima iscad anc otn adn heecn it proeisvd lusrc“rttua tncap”esoscm to eht oel,ganlc ei.. tup a knik in the plaha )e.ilhx fI yclnegi is lcsepmida yb niethogms ,eles I dt’on htink gnoplacrle-o cna fomr tis ctreocr rneyoasdc tuu.errcst
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