I ,rfgdeiu --yeXingcYl is alynctlchei nescodedri a pyarir“m oinam aidc utrsrtuec of a p”oenrit incse the nteiniodif of a maryPir eustutrrc of a oepnrti si “a naerli aihnc fo oianm s”d.aci fI oyu msse itwh eth ramrPiy u,scertutr sa ni hte nuotesqi ,tmse uoy ntaocn fmro hte oaSrncyed srtcrtuue fo the tn,eroip ihwhc si eedrdntmei yb hte gr-yohdnbodneign hciwh rcoscu weteneb the peipted kbcbaneo, eneiptdndne of hte R s.rpuog I pheo htis meda enes.s
morF akeidiiwp: dy“naoerSc ersruuctt si oraylmfl deedinf yb het traeptn fo rynhoedg sdonb neebtew hte naoim rodyhegn adn xlocabyr ygexno tsmoa ni teh dteipep nkeabcob.” pmiseash( min)e
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 sguy dan i eqotu orfm dtefteesl-/w/t:.noesm4oht/pilet1irpue/tgco.hstocea2smsawio/wcsbrrp0i
"09% have an dnlfiiieetba geitcne niatmout OC
L 11A nda OLC A12
eausc
s bomaalrn loelcagn oglsrnsn-ikic vai a cgnieyl stuinbotstui ni the glrleonpoac ceeoulml "
cwihh easnm htat IO ahs a leiyncg bsinttutisuo dan eoherrtf sit bluane ot orfm a ocasdreyn tusur.ucret
Deu ot ncligys'e lmsal s,zei ti tecsaer iksk"n" in the oainm caid qs.eenuec esThe skikn are ededne to tlrecycro ofmr eht cysdrenao turur.tcse
htOre :rnesswa
y-XlY-G is cebnokab for laclneog hapal cah.in 3 eoclganl lpaah nichsa aripls to omfr rpelit i.lehx necliGy hsa no R ugor,p waonillg fro tiifllyxibe adn tifrnomao of eltpir lehx.i No nlgiyec etvrnpes hsti nnctuosiou iagsrin,lp erpgvteinn eht mrofantio fo clangleo naerdycos sturerc.tu
lelRca hatt lhs-heieapcal dan sth-esteeab are seeaxplm fo ronsayedc eutc.strsru sThi nac be tuhotgh of a toanmtsfnaeii fo teh palah le.hxi
oehAtrN yaw to teg ta it is iva ole:iatnnmii
A. gynreohd inodgbn unowtdl lleyar naeghc sncei hitrene aiannle nro ylingec ear aBp .lor yGl g&;t alA hotlunsd' egncha who rinpelo si mdoifeid (I mean ti CLUOD, if hreet swa a cistre ndchniear or hieno,gtms but ont a etgar weas).rDn notghni to ndticeai htta llegocan airdgenetdo si aderetl in ersnsope to an AA tsiuuit.tsbno ,lAso in hte ontxetc of IO w(chhi is teh sieetnnrpg tilnpaomc,) we earaydl onwk ttha eth plobmer etnsd'o aehv ityhnnga to do twhi ei,dretgaond moer thiw eth hagcen ni ntEscut/frentuci. ruo elyonHst tond' wkon.
ee’srH neo awy to tlsafcrepmiseioe--on es“dracede debhg-ooydnnr of”:oiatmnr mI’ nto a igb afn fo isht lnie fo nionaers,g ubt tyccaehlinl ilnaane as a iesd uorpg hsa reom gn*ryeshod for tiltpoaen ydrgehon igbnnod htna eignlcy:
a:elanni H3—C
y:eilncg —H
,oS yci,nlthal“c”e ianlane douwl tprmie more rondeyhn-gdob ionf,trmao hcwhi gmtih lolwa you to etinmiael taht .ciehco
thaT sadi, it emsse oltams eplbiosmsi to leur otu ith(ouwt eyrv eccatinhl leneowgdk ro esmo peodirdv lmxerpnaieet dtaa) ttah eht ytiglhsl leargr aelinan sdoe nto rimpai gendyrho ognibdn neteewb agecloln cuesmoell avi srteci pl)ist(aa tefnniecre.er In mlpries em,rst cnesi nlaeani si e,grarl ouy owdul nhtik atht it muts wsoohem nreiertfe tiwh hte gyonhdbgdro-enin htat orccsu wthi teh -lpywedit nilyecg.
---
y*cirttlS gnk,espia is’t nto eth embnur of nsrgeydoh btu slao het ehrtngts fo eht lepdio tath citaastifel ygohredn ndni:bog a drhnoeyg dobnu to a tygsnlor eortcgeintlvaee lumloece ikel efloirun wlli ”“ppaera eomr tpeoivsi ,nad sth,u gnyd-odheonbr moer otsyrgnl whit a nayreb geyxon ead(opmcr ithw a gyehodrn cndnecote ot rocn,ba for e)apexm.l
reFhurt ndgraei:
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 gihtm be hnkioregtniv it utb, H bdno mooatfnir of a'sa emask the aycdenros uetsrutrc fo hte otrnpie oln(eacgl in sith c.)ase The yGl to Aal bunistutitos sdeo eutrls ni slse H nodb rnom,oaift tub fo aiundidlvi 'saa ton ebteenw engcloal meocuells tat(h itmhg eb eorm orf aaynrquert ecuttr)usr
aPmryir uurctstre = oiman cdia eSynenrae uecqcsod turerucst = rtuecustr edfmor wthi a esnlgi monai dcia neequces bae(t epdtale ,these apalh el,ixh a)cr tTeieytr srtcutuer = epliutlm esadcrnoy crsteuutrs irtcneigant rohetget (ptlliume baet ltedape etessh eksdatc no tpo fo ehac reh,ot )rQenacy trurate rturtcuse = ponreit utecrtsur deromf fmor ifolgnd fo lla rtieatyr ssruretutc to amke dgnbnii ,eisst .cet
cSnie the nilaean swa tup in pceal of het en,lGcyi eht airrymp rutuetrsc was nlaueb ot ormf an haalp exhli scnie aahpl xlhie crssrutetu eedn a trliracaup ncsequee (gly - x- y) in rorde ot form engyodrh odnsb to kepe hte iexlh s.ablet
tahw si gaecllno ? a androesyc poentir uutrect.rs
wenh yuo eveorm e,ycglni eht smto dntnuaba omnai dcia , rfmo eth ceursporr eeloclmu llwi yuo etg a prpoer ecsrndaoy eutusctrr ? NO
lyG si ,rlpao iaenAln si olanonpr adn h.doihpcybor eMesnsis nesornetavvconi otat.unim Teshe AAs veah dfeternif aclihmce peproirste whcih aled ot dtrisedpu trnpieo ognidlf d(cansoeyr e)cu.trstur ilriaSm ot luG - Vla niotutisustb ni cSikel Clel eiss.Dea
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$279$49I tnhki ti ash htnmsieog to od wthi gliyenc d(ue ot ist lsalm zies it can itf ni nmay lapesc hweer rhtoe nioma dsica anc ton nda ecenh ti svdieorp ur“satutlcr assctmcoepn” ot the gc,ollnae ei.. ptu a ikkn in teh aphal .exilh) fI elgnyic si lciamspde yb msgonithe ,slee I nod’t hknit -ancorlelgpo nca omrf its ctcerro osardnecy suurte.trc
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