I rufe,gid n-yicXelgY- is ntielcchlya oredniedsc a aprm“iry onaim cdai scrruuett fo a erot”pin sniec het otfnidinie of a irarPmy ruetucstr of a tiporen is “a relian chnai of iamon d”s.aic fI yuo ssem iwth het armriPy tet,rrcuus as ni teh euiqostn tsem, uoy oannct mfro teh acoSedyrn tctusruer of het oinrpet, hiwch si erteeddnim by teh nnen-rddhbgyiogo icwhh orucsc ewtneeb teh detpepi knobceba, pdeteinnden of hte R pgr.uos I oeph ihst aemd .seesn
mroF iewidikap: caydn“oeSr rcutertsu si faylrmol inedefd yb hte erantpt of ondhyerg sdonb enetewb eth omina gdeyrnoh nad lbaoxcry eynogx aomts ni teh depepit beanbokc”. ssia(mhpe enim)
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 yusg adn i ouetq rmfo s/gawiccpsots:/tsoedh4lh/ert-rbw0miif/pweuto.n1oetsr/teoecmapse2l.ti
0"9% aveh na aiinibldetfe inetgce inautomt
LOC 11A and LOC 2A1
seus
ca nolaambr ngclleoa kgrnl-csiiosn iva a leicygn sttubinsotui ni the nlaooclrgpe eceomull "
chhwi masen taht IO ash a yelicgn stibsontutiu nda otferehr ist nableu to mrfo a ydncsaeor rtrtec.suuu
euD ot sni'cyelg smlal ise,z ti rtseeac knisk"" in the oainm idac nse.eceuq eeThs nkiks era dneede to rctcleryo rfom hte onaycersd .rcrutsuet
etOrh newasrs:
Xy--YlG is kecaobbn fro aogcelnl lapha ic.anh 3 gnlolace lapah ihacns plsria to mrfo tirepl .xheli cnlyeGi hsa no R upo,gr lwlnoiag ofr fylxitbliie dna ntifomora of iteprl lx.ieh No igyelnc venspter isht outnusionc ilp,inargs eitnnrepvg teh rnioaftmo fo caolglen adnoycser .csrerutut
lcaleR atht icehahlse-pal nda setbehe-sta aer axemespl fo eacyndors sutecu.rsrt hsiT nac eb hgoutht of a ttoimnaienasf of het hpaal iexl.h
hoNetrA way ot teg ta it is iav n:imnioliaet
A. noregydh ndnoigb wlnodtu lyrale cneahg eincs ritneeh anlniea rno nclieyg rae oBal.rp Gyl ;&tg lAa tlhdu'osn hcgnae hwo oplneir is deiifdmo I( aemn it O,UCDL fi rheet was a tcries hcnadenir or nghomte,si tbu not a rateg )saer.wnD nngohti to decniiat thta leaoclgn giddteorean si dearelt in esesrnop to na AA .tsitsnoutbui s,Aol ni the cxontte fo OI hhwic( si eth nesnriptge cima),onltp we yraaled wkno that the lorebmp s'neotd avhe ihagnynt to od hwit d,nortegaeid rome wthi het neaghc ni u.iuErc/ts notcetfnru nloyesHt 'tond onk.w
eres’H neo wya to ainfreesmpscieloto-- edcsera“ed nobr-eondghdy oira:mtfn”o ’mI ton a gib fna of ihts nlie of ornigas,ne tbu lntyihelcac laainen sa a dies pguro sha ermo yn*desgohr rfo pttlaonei eonydhgr bgnonid ntah ecyngil:
:ienalna 3—CH
cyelnig: H—
o,S in,atylche“l”c eiannal dwuol rptime rmoe ngoyodn-dhreb mirtfn,oao chiwh mhtgi walol oyu ot neamltiie ttah .ccheio
Ttah si,ad ti sseme mlsota mlosisipbe to elur uot wih(utot rvye cncaileth nedeowlgk or esom rdpdiove neailrtpxmee dtaa) htta the syliltgh lagrre annaiel esdo nto airipm rhgodyne dinnbog etewneb clongael lulcoemse aiv criets ptiaals)( .fencetreienr In rmlpeis tme,sr necsi nineaal is laregr, yuo ludow nkiht tath ti smtu sewhmoo rtieeenrf thiw teh bngdinyohoedgr-n ttah rsccuo htiw het w-ydtpeil cgeiyln.
---
ttrSy*cil epnaig,sk st’i ont hte buermn fo hoygsnrde btu olas teh ntgrshet of eth dipleo taht sattfceiali hdyogner nigdob:n a hygerdon nodub ot a rytlgons iltocveageetrne eecmlulo keli uiofnler llwi e”praap“ erom vspoiiet a,dn uhs,t g-dyhoeborndn omer gsronytl itwh a brenay xygoen p(mcdareo hitw a yndehrog odetencnc ot bna,cro rfo elap.xem)
rretFuh irnged:a
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 ihtmg be ovinighertnk it tbu, H bdno oimrfaotn of saa' askme het ynoacrdes uutrtersc fo the ntiepor c(laelong ni siht ).aesc The Gly to Ala inotiusuttsb deos urtles ni ssel H odbn imf,rtaono ubt fo idnaiivlud 'asa ont eeetwnb elacglno lmlseceou (taht tigmh eb eomr fro tarqyeranu tcetsru)ur
rayrmiP tutcsuerr = oanim diac yaeoS ncnreeduqecs rucsutert = srutcrute fedmor htwi a sgneil onmia dica esqceneu tba(e ateedlp sheet, aphla le,hxi crteetraTiy) rutesctur = eputmlil yasndroce teuursrsct rangiteticn ottehrge itlpmuel( eabt etlpade thsees caksdte on otp of ache ehot,r ruetQr)ctanre ya crrseuutt = ptonire rtuuetrcs frmeod fmor gfnoldi fo lal ttrryaie tsrteurucs ot mkae gnbdnii sst,ie etc.
iSnce eth anenali asw tup in calpe fo eht iy,Gcenl eht myprrai tuectrrus swa balune to frmo na hapal ilhxe since hplaa lixeh ctsuetrurs deen a trliacrupa unqeesce l(gy - -x )y ni roder to mrof ohryegdn bdosn to ekep het leixh stbl.ae
htwa is gcaellno ? a dayneosrc ptnorei rucrs.uett
nweh uyo merove le,ngicy het toms nudtanba mnaoi caid , fmro the scprorreu leuloecm liwl uoy gte a oerprp nreaycsod ustcuetrr ? ON
ylG si oparl, naiAeln si ponoanlr nad .drihpoybhoc sseMseni tvocvanesnnieor outm.itan sheTe AsA evah ridnfftee ealcicmh etpirersop ihchw dlae to stprddieu eripton nglfido aoedc(rnsy su)r.rtcute lSmriai ot Glu - aVl ttsuioibnsut in ckliSe leCl aDee.ssi
submitted by ∗wasabilateral(47)
It can be re-accessed by making a purchase.
Purchase your membership here
$279$49I ihtnk ti sah nstgemohi to od htwi ycleign (ued to sti lmlas isze it nca tif ni myna lpeasc rhewe treho oinam iscad nca nto and nhece it preisdov tr“lcsuruta scptsoe”anmc ot het eg,llcaon .e.i upt a kikn in hte alaph .e)hlix If lgciney si csapmidle by nhisotmeg s,ele I ’tond kinht rnlgpeooal-c anc rmof its ecortrc acnoesryd uurecsttr.
$279$49