I i,fdrueg Ye-ngliXc-y
si ilteylchnac ndesiedcro a ri“yrapm aoinm acdi tecursrut fo a irtoen”p eicsn eht nideoitfin fo a aymrPir reuuctrts of a pietorn is a“ aelinr canih fo imoan .sai”dc fI yuo smse tihw eth Piymrra re,utrtscu as ni teh tesioqnu s,tme you oantcn ormf het narecSydo ttsurruce fo eth tr,ineop iwhch si ietdredmne yb eth oinnyhegndgbrd-o hichw crcous bweteen hte dtieepp obenkcba, tiednenpnde of hte R pro.usg I opeh ihts adem .sesen
rmoF keiapdiwi: ecdnoSra“y usecttrur si oraylmlf deedfin by eth tentapr fo gdheoynr dosbn beetwen hte mniao egnohrdy and lxyorcab xgenyo motas ni het edpteip bcoakenb”. ipme(sash mn)ie
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 usgy and i eqtou rofm 0pmebtoicrsetw:1wletrssaplo/fctru.t-e4idess/ho2iewm//aoo/set.tcpinhg
"9%0 ahve an dfniletiiabe giteenc attuoinm
COL 11A nad COL 1A2
cs
esau nbmlraoa clgeloan is-nogsclkrni vai a gelnciy itsusiotbnut in teh alogceopnlr muleolce "
cihhw asnme tath IO sha a egicyln souitbnituts dan hteefrro ist lanbue to ofmr a radseonyc t.uuucetsrr
uDe ot yn'eilscg mllsa sez,i it saretce k"s"ink ni eht nimoa caid su.ceqnee eTesh kisnk aer eedden ot etccylorr omfr het royeasdnc tc.tusreru
hOetr ewssnra:
Y-XGly- si bebonack rof ocanglle aahpl c.hnia 3 egacnlol ahlpa hisnac lapirs ot omfr eriltp x.ileh cnlyGie ash on R grup,o alwlnogi for iblxyitelfi and atnoifmro of teilrp ei.hxl oN yenilcg tvsrepne stih ntncuiouso lrgnipas,i ngivnerpet the noitfarmo fo gaclonel daoencyrs ctesurtur.
Rcaell ttha paacehehllis- dan tse-bheeats rae plamesex fo drycnoaes ctutrressu. Thsi nca be uohhgtt fo a mtnaitfaiseon fo hte hapal x.lieh
AhtreoN way ot etg at ti si iva iliiam:netno
A. deonyrgh inodbgn lnotdwu aleylr ecnagh icnes tieehnr alnanie rno yelcgni aer l.ora pB yGl &tg; lAa s'duolnht ngchae woh rnopeli is fdmideio (I mean ti COD,UL fi ehret aws a scteir cirnahned or sgnhte,oim but not a etarg ren.)saD w ntnhoig ot ntedacii ttah alncogel groidtndeae is dltaree in eeopnssr ot an AA tuinbosut.sti os,Al ni eth cxottne of IO cwhih( si eth inpgesetrn )nilc,mpoat we yrldaae wokn htta eth bleorpm osnetd' veha nithagyn ot od wiht goedaenr,tdi rmoe iwht the ecghna in ucrEuu.tt/ei fcntorsn estyHlno n'dot kw.no
H’rees neo awy ot reosint-eco-mfpeails eces“dared oogrybhddn-ne nt:oamf”rio m’I ont a big fna of thsi neil of osnr,ienga ubt hylcaieltcn aleinan
sa a esdi rguop ash emor hdseyn*ogr for tpiotalen gynohdre nindbgo athn ceyngli
:
el:nanai
—H3C
le:ngyci
—H
,oS ayl“”chctenil, ianlaen
uoldw emiprt rome odrbgeyd-nnho itfaoro,mn cihhw hitgm alwol oyu to meeatilin hatt .ehccio
Tath ,isad it essme mlatos ssimbiploe to urel uot tuoh(itw yrve nilacehtc egleokdnw ro osem predvdio partemxileen )adat ttha het ihltylsg reragl lanniea
sode nto mariip orhegndy ngdniob etbween loagenlc smcleeolu iva cresti lpaats)i( rfnncetieeer. nI mplries ,mster ncsie naliaen
si lerrg,a uyo uodwl nihkt htat ti mstu omehows ierertfen with eht gnio-hegnrddnybo ttah crucos ihwt the ydeltwip- lniygec
.
---
ticS*tlyr isn,gaepk tis’ not eth nburem fo rhsgdeyno tbu losa the rseghtnt fo teh pedloi thta litafsticae deygrnho nobgni:d a egrnyodh ndobu ot a roytgnls inlegatrceeovte cemlloue klie erfloinu lliw ”aera“pp mroe iitsvepo adn, tu,sh dyornngoheb-d remo gnyrostl itwh a nearby engxoy ed(raompc htwi a ogeryhdn dncoeectn ot nr,cbao fro el.apx)me
urhtrFe dnge:rai
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 hitmg be nkintgrehiov ti btu, H bodn moirofnta fo sa'a eamsk het ernydosca rtsetucur fo hte eirtpon (lcgnaeol ni tshi a).sec eTh yGl ot Aal iisttubsotnu sode sulert in sels H nodb f,onoirmat tbu of ianvliidud as'a not tbeneew lalgeocn mlsloueec tat(h hmtgi eb oemr rfo erruqnatay rrcetut)su
yriPrma cuttrrseu = manio daci eSsenreeunqyc oadc tcsruertu = rrsttecuu femrod whit a eisgnl minao daci ensuceeq ebt(a ldaetpe eetsh, halap ielh,x aTertric)yet ctuutsrer = illtmpue nrodyscea uecttsrrsu rninttgeaci etheortg (muitepll eatb eeapltd thssee ascdtek on tpo fo aech o,rhet rrrntyeeacut) aQ sctuutrre = iorentp rurtuctes dfemor mofr dlofnig fo lla etryiatr rusursctet to akme idgbinn etsi,s .cte
Sinec het ailanne asw utp in epcal of hte yG,lenci eht yrirmap srrueuctt was luanbe to frmo an lhapa ehxli sicen hapla heilx erstcrtuus eedn a crlautipra cnqseeue y(lg - -x y) ni drore ot frmo ohgynrde sndbo ot ekpe hte lixhe t.labse
wtha si nacgeoll ? a nsycdroea ipreton .uurcertst
wehn ouy evomre ncl,geiy het omts tanbnaud oamin dcia , fmor het prsceorur cllumeeo illw you gte a eprrop rseoancyd etrrtscuu ? ON
lyG si ,rpaol nlnieAa si oonrnpal adn chhrod.bopiy isMensse rnitevasoecvonn tnitoma.u eTehs AAs ehva ftiderenf lhcmaice espotprrei hwhci aled ot sdprdtieu rnpoite idlofng d(acesyrno csrr.uu)ett riilamS ot Glu - laV usitibttsnuo in iecSkl leCl ase.siDe
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$279$49 65% OFFI tinkh it ash shgmeoint to do whti inycelg e(du to tsi mlsla iesz it nac tfi ni mayn sclpea ewher toher nomia isdca cna tno dna hcene it veosirpd srt“uluactr msas”ceptocn ot the agolnlec, ..ei tup a kikn ni eht hapla elhix.) fI eicnlyg is dcpilaesm by hesmnotgi l,ese I n’dot tknih lar-ecpnolog acn form tis ecctrro conesyrda stter.rcuu
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