I ,difurge g-Yylin-Xec si claylihtecn secidderon a rpa“yrmi aiomn icda csututerr of a eon”itpr iencs the nidfointei of a imyPrra utetrrcsu of a rpeitno is a“ reinal chnia fo ainmo is.”acd fI ouy esms iwht hte aiPrmyr etrsu,rcut sa ni the snuetiqo t,ems uyo taocnn rfom teh ocdyarnSe ctsteurur fo eth rotpine, hcihw si tnddeeiemr by eth -nbynorighedngdo cwhih cocrus nbetwee eht ieedppt obcbeakn, npnedtdneei of teh R rousg.p I ehop iths eamd nsese.
Frmo kdewipiia: Scyaron“ed rtuuesctr is yrofallm deinefd by hte tnatpre of ynehrgdo nsobd nwbetee eth imano drhogeyn dna loxyarcb egynxo osmat in eth etipedp cnbabeok”. ise(mhspa imne)
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 gsyu dan i uoqet ofrm s/rlhpfiwge.et/lau01sowsciip4:ohstwsooret/tte.-atbm/2meepcscdotr/nie
9"%0 evha an bitiaedeilnf ignteec tauointm LC
O A11 and OCL 12A
eas
cus braoamnl cganlole ncrn-liksgosi aiv a igcelyn uiubsntistto ni teh oapnolgcelr coleelmu "
whihc esamn ttah OI hsa a ilcegny suiottibusnt nad rreethof ist leuban to omrf a yeondcasr c.uutetusrr
eDu ot lns'cgiye lmals ze,si ti tseacre "knkis" ni het moani cdai .esncqeeu heeTs nkkis are endede to ycltrroce mfor the dosacrney rte.urutcs
Otehr se:srwan
X-GY-yl si baeocknb for nllcgeao lapah a.ihnc 3 llanegco phala ahcnis psialr ot rmfo eltirp elix.h leyicGn hsa on R ,pogru lilwgnao rof txbiiyleilf adn tioorfnma fo rielpt lexi.h oN ylgecni eevrspnt shit ntisuucnoo ri,naslpig eiprentngv hte orntiafmo fo laglecno radyecson cesrutur.t
celaRl ahtt ilh-eeapashcl dna tetehsbsae- aer splaeemx of roneadysc turssur.tce ihTs nac eb utohgth of a aatnmitfeosni fo the palha x.hiel
eAhtNor awy ot etg ta it is iav omtiiielann:
A. nyderohg dginnob wtulnod ryalel gcenah scine rhetnie anilnea orn gicyenl rea rpola .B Gyl tg&; Ala tnus'dohl ghacne ohw plreoin si efmioddi (I anme ti LC,DOU if treeh swa a restic danrcnhei ro m,sntgoihe tub ton a garte nasD ew.)r tonginh ot aicdenti taht clengloa aredigedotn si raeldet in rseeposn ot na AA onsbi.ttuutsi olA,s in teh ctxeton fo OI ci(whh is het engnrtpies ,atomlp)nci we adayrle wonk hatt the emobrlp nt'sode veha itanyghn ot do htwi rdgntedeia,o rmoe htiw the cganhe in ue.tcEutrn ioufcrts/n onetyslH nodt' kwno.
eHe’rs one way to li-spetaoco-renmisfe ardecs“dee bdonenrgh-yod r”mfon:oait mI’ otn a gbi fna of sith inle of nrg,eoinas ubt cehnylailtc anilnea as a ieds uporg sah eomr hgeros*dny for aneotiltp ehorygnd niognbd hnat gecnliy:
:lnneiaa —3CH
g:eincly —H
oS, ylnihaelct,”c“ aelnnia duowl repimt omre yenonrd-gbodh riotao,nfm chwih ighmt owall oyu to ntamieeli htta ccie.oh
thaT dasi, ti esems omlats miobilseps ot uelr tuo t(htwoiu eryv ihnccetla ewdleokgn or emso ridpvode eraeietpxmnl aat)d ahtt eth hitlylgs reargl ieaannl dose tno prmaii yoendgrh boinngd tbeewen enolclag louclseem iav rtcesi til(p)asa ntenec.reirfe nI mspirel ,terms escin aelnnia si ,alrerg ouy ludow kitnh ttha it sumt ohswoem ifreenret tiwh hte gbenoniddyr-hgon tath csuocr hwti teh -dtewpyli glincye.
---
itlScr*ty ,aegikpns s’it nto eth mrbuen fo rdhoynesg ubt aslo eht esntrhtg of eht eipdlo htat acealifstit ohedgnyr :nnbidog a groynehd bdnou ot a tlsonryg ceertevegoitlan leloemuc ilke finreuol illw pearp”a“ oemr pivtesio ad,n hsut, oh-ygebnnrdod meor ostyrlng with a rnaeyb yxnoge ocpear(md hwti a ohngyder cneedoctn to ocbrna, fro p)exaem.l
uFerhrt ngadei:r
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 gmiht eb gniokhrnetvi ti ,tbu H dbno oonfaitrm of as'a emaks eht caryednso urctuesrt fo eht irpoetn oe(gallcn ni siht as)e.c Teh yGl to Ala iittsnsuuobt oeds trelus in sles H dnbo arfot,iomn tbu of avlindidiu aa's nto teenbwe gcelonal eueomllcs tath( gtihm be moer rof tayraqeunr rrtse)cuut
iaPrrym etcrtrusu = imano dcai ede qaynuceecsnrSo rruectstu = cserrtuut foemdr htiw a sigenl aonmi aicd eucensqe aebt( leeaptd e,etsh ahapl elx,ih yicatrertT) e ruttscuer = ptluemli odesnrcay ustsrucert trngeitainc ehrttoeg eitmllpu( abet paetdle hetess ecstadk no pot fo chea ther,o y carQt)reaunert ecruutrst = oieptnr rttusecur fordem from lfdgion fo lal rettiray ssruurtetc ot mkae indbgni est,is tce.
Senic the aennlia asw tpu in alpce of eth Gecn,liy eth ampyrri esrrutcut swa eualnb to frmo an lhpaa ihelx cnesi phaal hlxei usrtetrscu nede a iurptcraal uqesecen (ylg - x- y) ni order to fmor ehrodngy bnsdo ot ekep eht iehxl bealts.
waht si aneglclo ? a serdonyac itrneop sr.ucrutte
when uyo evrmoe eclnyg,i hte stmo dntnbaau amoni caid , form het urrcpores eclmelou llwi oyu tge a eprorp racosdeny rutsructe ? ON
ylG is ap,rol ienalnA is aopnrlon and opihobchr.dy esMniess screntnvoenvaoi ti.uomnta Thsee AAs aevh erietffdn alhccime ieeprrspot ichwh elda ot ideupdtrs inptore gofndil nrcde(asyo euc)s.rttur rliiaSm to uGl - aVl uosbtnisiutt in cSelki Clel aesDse.i
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$279$49I thnik ti ash gsithonem to do tihw lneycig e(ud ot sit lmlsa zise ti cna tfi ni many lecpsa ewrhe eotrh imona isdca nac nto and ehcne ti rievpsdo c“turltarsu onps”saeccmt to hte g,ocenall ..ei put a kkni ni the haapl hiel).x If gyeicln si ieslcdmap yb tehnmgios ,sele I d’not htikn alpnrlgce-oo nca fmro its rctcroe edsnyaocr ts.urcteru
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