I e,rduigf --eYlcniXyg is lnileycacth oernsicdde a prr“aiym oainm iacd tterscuur of a p”neoitr escin eth fiiendtoin fo a yarmPri ttscreruu of a toenrip si “a rnalei nicha of iaomn csai.”d If uyo sesm htiw het rmPiary tt,ueursrc sa ni eht squineto es,tm oyu noncta from the yeScarnod rtscrtueu fo the iope,trn hcwih si rtdeiemend by teh deng-dgonbioyrnh chwhi rucocs weeenbt teh ptiedpe bcnkbeao, pnddeenniet fo het R .sogpru I hepo shit dema esns.e
mrFo adpkeiwii: “aocdrSeny rrtestcuu is aymofrll ednfdie by eht epntrta of eyrgdnho dsbon eebwetn eth manio deonrhgy and xcryboal ygxeon tosam ni teh epepdit aokbnebc.” saihmpes( mi)ne
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 suyg adn i tuoqe mofr ushhpr.g:/0/rso/wleoemaec2tiirttpm1lwosesta/foe-decscbinwep4.totits/
09%" vahe an idlnfeiabtei etigcne tuatnimo
OCL 11A adn OCL A12
asecu
s nraaobml anglolec nsioslrcng-ki vai a ilcenyg sottsiuubitn ni teh ooelnlgrpac eelolucm "
which esnma atht OI ahs a ligceny oiitustnutsb dan ofrether sti leaunb to mfro a yranseocd uects.urutr
ueD to 'lecysgin llmsa se,zi it eesartc ksnik"" ni eth onmai idac eceqe.usn eehTs kikns rae eededn to ltycrcore fmro teh ydeanoscr rstutre.uc
htOer :sawrens
X--YGly si ocanbbke rof noagllce lpaha cai.nh 3 eocnllag haapl achsni alprsi to rfom lpetri xih.el clnyGie sha on R g,ropu awgnloli rfo bflexiliyit nad oftaomrin fo trlpei hxlie. oN ginclye pntrvsee thsi stnuocunoi iai,pnsrlg ngpnrvieet het irofntoma fo celogaln eocdasynr rrucett.us
laRcel hatt h-epehilaacsl dna tt-haeesebs aer pexeasml fo yaodscrne cttuerssu.r ihsT nac be houhgtt of a easiintofatnm fo eht aahpl hil.xe
eAortNh yaw ot gte at it is vai tioienna:lmi
.A ehygrnod dbgnoni woduntl yerlla ecngah secin trneieh aalenin orn lcyiegn aer oplr.a B ylG gt&; laA 'duhnotsl ncgahe hwo ielnpro is eimfidod (I mnea ti DCOUL, if htere aws a trscie naihdencr ro eishnt,gmo utb ont a raget aw)e rDns. hgionnt ot dictniea atht elnogacl neideatordg si rdteeal in nrpseeos to an AA n.uiusiosttbt Aosl, in het ntecxot fo IO icwh(h is the girptnnese aml)otpi,cn we aaredyl onwk ttah eth rlobmep tdse'no vahe ihngtany ot do wthi ergt,deiadno eorm iwht the echnga ni n ctutioEe/rufucts.nr eonysltH do'tn own.k
esHr’e oen way ot -sn-ateofsiclieoepmr eraedcse“d oyo-drnghnedb :aonmr”iotf ’Im not a igb naf fo htsi eiln fo iannsger,o ubt ichelaclnyt aialnen sa a sedi porug sah erom *rdygsohne rfo oletptina ygornhed gdnnibo hant lyneicg:
i:lnaean H—3C
:ieynlgc H—
oS, “ahillytcen,c” naalien owlud mitper rome ynbrdgdne-ooh imatnfro,o whchi gimht aolwl ouy to leieamitn thta cc.hioe
thTa a,dsi ti esems stlamo pimbilseso ot lreu uot wouit(th evry tncheical okewgnedl or osem ddprvieo erxnteeialmp a)adt ttah eth tglshyil raelrg alinane sdeo nto arpmii rhogenyd onigbnd betenwe olngelac ulmeclose iva reitcs tal(si)ap eeitre.cnrnfe In pmilrse tem,rs icens ianlnae si e,rlrga you lodwu thkin ttah it muts wosemho rineretfe itwh the gebryon-ghnioddn hatt crsocu with eth t-lyidwep ceilgyn.
---
tyiSrtcl* enskagp,i ’tsi otn eht rubnem fo rnheodygs but oals eht htsrgnte fo teh eilopd ttah efliiattacs dgnehyor g:bdnoin a oenrdghy ubdno to a glynsort neogartteiclvee lmueeloc ekil noierluf lilw epara”p“ omre otipeisv nad, tuh,s egn-yrdhonobd reom ntyglosr hitw a eyanrb gxoyne pod(cream itwh a rnogydeh etdccnnoe ot arcnbo, ofr epea.xlm)
rFeuhtr rea:dngi
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 higmt eb girkovnhtien ti u,tb H ondb faotnirmo of a'as kmsae het ndyrescao rturuestc of het nprtieo gal(cenlo in hist .)sace hTe ylG ot alA oiissutbuttn seod slretu in sles H obnd roaiofnmt, ubt of iailuvdind as'a ton nbteeew nelgocla oluclmese (atth himgt be rmoe fro qetnuraray returcstu)
yrraimP tsurertuc = aoimn iacd yu eeSanrconqcesed tscuruert = utrscetur morefd thwi a igsnel miona adic cuqneese (eatb delapet t,seeh aphla l,ehxi rietcTeryta) ucttresur = metpillu doacysnre setrrtcusu iagtnncriet ettgoehr eptll(imu eabt eptadle tseesh ckstdea no tpo of chae r,htoe te)Quryecarr tna urcestutr = eptnroi tetucurrs foedrm fomr nilfodg of lla trtyerai reusttcurs to aemk diignbn tises, .ect
Since teh lnianae swa put in aecpl fo hte cn,lGiey teh mrpariy rsrutuect wsa nalube to fmro an aphal hlxie nisec lhapa exlhi tcsreuutsr dnee a raciptaulr ceesnueq gyl( - -x y) ni oerdr ot fmor odynherg nbdos ot epke hte exhli a.tblse
wath si naoelcgl ? a oersncday ronteip .uttcuersr
hwne you meoerv glcen,iy hte smot atnndaub amoin idac , ofmr hte pcruresro celomeul illw yuo etg a reropp odesrnacy secuurtrt ? ON
yGl is raplo, eAaninl is lnnoorpa dna p.oycibohrdh ssseinMe iscnoreonavntve ua.ntiomt seTeh AsA aehv rfeitefnd claemihc petporrsei whihc eald ot pseitdudr tponier odgnfli snoyacdr(e t)esrruct.u mlSaiir ot ulG - Vla sstitubtunoi ni ciSkle lleC sai.Dese
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$279$49I kinth ti has onmgihtes to do htwi gceilny (deu to its mlsal siez ti anc tif in nyma peacls eewrh rtoeh imano dsaic cna ont nda ecnhe it irpesovd s“ructualtr pssm”cceaont ot eht agclnol,e .e.i utp a nkki in hte lpaha il)xh.e If yegnlci is lcpmiaeds yb stmneiohg ,lese I dont’ ithnk logroecnap-l anc rfom sti rreocct ceosarnyd eu.utrrtcs
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