I rgeifud, Y-gnlc-Xeyi si ciyalcelhnt inerodcsed a myriar“p omani cdia utrctersu fo a ine”ortp insec hte iindeotinf fo a yirramP teurrcuts of a neptrio si “a eralin nchia of nmaio c”d.sai If oyu sesm wiht the mayirPr ,usutrcrte as ni teh sntoiqeu ,stem ouy actonn frmo the Syceanodr uurttrces fo the npti,ero hchiw si rtmeeinded by het idhggyonendno-rb iwchh sccrou ewteenb hte ptdeiep nkebcboa, ienndedpnet of eht R g.rspuo I hpoe sthi aedm sesen.
From kpwdiiaei: edcaSo“nyr eusurtrtc si mlyaofrl nfdieed by teh tpnaert of ydorgehn nsobd ebenwet eth aoimn enrydgho dna yxlabrco nxgoey amsto ni hte idptpee baebknco.” shai(emsp m)nie
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 ysgu dna i toeuq rofm mnl.eioriupfot4/pede/ht-ewht2trie1i:smt/e.toassclspwcro/coge/sb0sawt
"0%9 eahv an ieenfitlaibd gcnetie notituam L
CO 1A1 adn COL 21A
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mroalban lglnecoa k-nssiolirngc vai a gycinel tttsiusibuon in teh oopaclnelrg eolelucm "
hwhci anems htta IO hsa a incgeyl tssnoubuiitt nad hrtfoeer sit ebluan to fmor a syonrdcea tutrr.uucse
Due to lsgyc'nei lmsla es,zi ti acteser ikn""sk in the monia caid cenus.eqe Tsehe kinsk era eednde ot lrtyeocrc mrfo teh yeadoncsr retrcuu.st
Oterh sne:wsar
X-lYGy- is bbknecoa ofr ceoalngl alaph cnhai. 3 agnleocl haalp saichn iplras ot omrf erplit hil.xe nGeicyl ahs on R ,pgruo nagliowl ofr yilbtfixlei nad orfamotni fo itrpel e.lihx No inyglce pnrvetse tsih inotsuucno gilp,sanir irgnpnteev the roamtifon of llenaocg ndsaycoer sctrt.euru
Ralcel htat lpelsaahci-he nad aeshesb-tet rea exlsmaep fo acnyoedrs s.etrsturcu sThi anc be tohtghu fo a nfoatnsatemii of het apalh .hxiel
rNohAte ayw ot get ta it si via onetiin:aiml
.A oreygdnh gbidonn notudwl lleayr gnceah cnies nritehe nnaaeli nor yilgecn are op. rBla ylG t&g; Aal 'tnsohlud ghance owh lnropei is ifemddoi I( nmea it DCLOU, fi ehtre asw a tcseri hdnearcni or sotnmihge, btu ton a rgate a).D wrens gohnint to aitdcnei ttha glnoleca rgeiddetano si aetedlr in opssreen ot na AA suiustboti.nt lso,A in eht xceontt fo IO (hwchi si eth nitsgnpree tlaonic),mp we yreadal wkon atth teh morpbel 'neotsd veah anghitny ot od whit ortndaedegi, mroe hwti hte change ni cctuure nsir/E.tfuotn nyoetslH ndo't ow.kn
er’sHe neo yaw ot ailfoeesprco-ntesm-i c“seareded bndgrhynood-e ”oimafton:r I’m otn a igb anf fo stih nlie of eri,gnsoan ubt ncalctyhlei ileanan as a esid grpuo ahs eorm osgne*dhyr orf poetlnati eogndhyr inogndb hnat yngielc:
:naelain H3C—
:ielcgny H—
,oS t,ie”lhnc“ylac lnnieaa loduw iprtem reom oodb-hndgyenr iao,fnrmto iwchh himtg llowa yuo ot metaelini htat ecicoh.
Tath as,di it essme tsmlao esopliimbs to uelr otu hitwou(t eyvr acnelhict egnwodelk ro emso redvdoip inrlepetxaem tada) hatt the yglhtisl gaelrr ilanean dseo ont mpiari enyodrgh onbnigd wetnebe eolcngla oleumelsc vai retcsi ()slptaai .rneteenecifr In lspeimr terms, eicns nienlaa si glra,er uoy lodwu nithk tath ti tsum eomshow ietfrerne iwth het onnndybe-igrhgdo tath crsuco htwi teh dlypiwt-e cginyel.
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*cltSrtyi p,gsnieak ist’ nto eth rnubem of gyhsrdoen tbu also the nhtertsg of hte oidlpe ahtt escalitiatf gyordhne gdobn:in a nyghedor oudbn ot a otrygsln releaevgiectton leoceulm liek ioluefrn will par”pe“a mreo spoietvi d,na hs,ut dneonr-oybgdh moer srntoylg whit a raneby gxneyo erap(cdom ihwt a eyrnghdo deetnncco to car,bno orf mp)xal.ee
etrrFhu edin:gra
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 itgmh eb gntrnioehivk ti bt,u H obnd mnaoftiro fo a'as keams the rydecaons sctrueutr fo teh iotepnr eclgola(n in hsti cea).s heT lGy to Ala bsuiiuosnttt odes eutrls in less H ndob firnmoao,t but of uadiviinld saa' tno eetenwb clnaeglo emlucselo t(ath htmgi be rmeo for uanrtryaeq rsutrtec)u
Pyairrm trctsurue = amoni adic noseceSerdqeauc ny reructstu = tstecuurr domefr iwth a eilgns naomi daci eeqncues bt(ae dpeelat ,eeths alhpa ,eihxl rraty ee)Tcit rtutrusec = pmteilul caedsnory ucttrsseru ragiteinnct rgtehtoe e(uimlptl etab tdpleea teshes etkscda no opt of heac etoh,r nrcut)ae Qeryart ctturrsue = irtpneo urtsuectr erdmfo mofr inlgodf fo all eyattrri cstuursetr to kmae dnbingi ,sties ct.e
nicSe the alnaine aws tpu ni claep fo teh ,clneyiG the maipryr utsrceutr saw nlabue to rmof na lphaa lhexi ceisn alhpa lxhei cruersttsu dene a urtlpraica eensuecq gly( - -x )y ni orrde to fmor dehgnory onsdb to pkee eht helxi sae.btl
what si cenoallg ? a ocdysrnae ntropei c.urtrtseu
whne yuo rmeveo gnlycie, het msto andunatb omian daci , rofm teh opsrcrreu oecemllu will oyu tge a poerpr neaycosrd cruesttur ? NO
ylG si oa,lrp lieAann si lpoornan dan hdooch.rpiyb sseiesnM tisonneonvevcar .utoinmat hseTe AAs haev tifndefer hameiclc terproeisp hihcw ldea to suitepdrd enitorp ldginof aocyrsnd(e ursrtte.)uc Smlriai ot Gul - aVl stsibuotntui ni leSkci leCl .eeasDis
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$279$49I kinht ti hsa ntghmoesi to do itwh ceyinlg edu( to ist mllas zsei ti acn fti ni many alecps wehre reoht nomai cidsa acn nto and ehnce it rpvoiesd caltru“tsru smcsepac”ont to the clon,ealg ie.. tpu a knik ni het aahpl .eh)xil fI iycngel is mplscaide yb hnsiemtgo ee,sl I dtno’ ikhtn gelpcrlan-oo acn orfm sit rcreoct aescynodr su.rtutcre
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