I igd,fuer nycYe--glXi is caytlhnclei dcenoeidrs a ri“apmry nomia caid eutrurtsc of a etroi”np necis eht nniitdfeoi of a ymriPar teruscrtu of a enporit is a“ narlei nahci of nmiao cas”.di fI you ssme thiw eht iyPrarm utcr,eustr sa ni eth qoisntue tms,e oyu acnnto frmo het ycenraSdo steurrctu of eht ,itponer hichw si rdtiemdeen yb hte gdih-ygneboonrdn whihc csorcu tnebwee the eipedtp cekabbno, ntedeinpden fo hte R grps.ou I opeh isht emad sen.se
Frmo edkwpiiai: “ndyreSoca uuttscrre is flyroaml dneifed yb the taetnpr of enhgrdyo obdsn ebteenw teh anomi oreghnyd dan bcrxoaly yeogxn osmta ni the pteidpe ckbaobne”. ms(aseiph )nemi
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.
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%"09 vhae na linatiidbefe gteenic itotuamn C
LO A11 adn CLO 1A2
s
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chwih snmae hatt IO ash a lncgeyi ibtuisstuotn adn retferho tsi baenul to rmfo a onsyrdace rsctu.urtue
Due ot egsyil'cn allsm ezi,s ti tecasre "iksn"k in teh oanmi acdi .ecsnuqee Teshe kniks aer nedeed ot oytrerccl mfor hte yasnodrec suttcr.eur
Otreh snwes:ra
YXyl-G- is akecobnb orf oegcalnl paahl i.chna 3 cegonlla lpaah nacsih rlspia ot omrf preitl xhil.e liGynec ahs on R gopur, wligaoln rfo ilbxtiyfeli dna oritnaofm fo rpilet x.eilh No ygcinle ernpestv stih nosinouctu g,rnislipa veepngntir eht rtmanofio of celaolng ncrsodyea ttr.ucusre
lelaRc hatt -ahsacpehllei nda t-shsatebee era esmalexp fo royendsca c.tutuessrr Thsi cna be hhgutto of a aitasmnteinfo of teh lpaha i.elhx
hAortNe way ot etg at it is avi na:lioinmeti
A. ndyhrgoe gnbndoi dwtunlo eylral gncahe scnei eerinth neniaal onr ycnelgi era B oapl.r Gly ;> Aal hst'ulndo gehanc ohw lrpeoni si diomeifd (I amen it LC,UOD if reeth asw a rtcise rncehdnia ro gemnisot,h tub otn a getra nrD eas.w) igohnnt ot einacdit tath enllcaog dtgeoairden si deltear in nesropes to na AA nsutt.toiisbu ols,A in het txnetco of IO wc(ihh is eht ntsgnpreei ,lanicoptm) ew dayrela owkn ttha eth oblmper tods'ne ehva ihnatyng ot do itwh i,tdeeagdnro rmeo iwht hte ghacen in ./ttuutrcsfueoncnr Ei esHotynl dtn'o ok.wn
Her’es eno ywa ot scsaoelo-emeinpti-rf ce“adeesrd obry-ogehddnn ifrn:motoa” Im’ otn a big fna of isht enli of eiaonrnsg, tbu lthyeicncal nlieana as a esid rgupo ash meor gohsredyn* rof ltitapnoe negohyrd ogndnbi ahtn ynlgeic:
n:nalaei 3—HC
ignlc:ye H—
So, l,nahycl”“itec ailnnea oduwl rpmeti roem bredhnd-gonyo notiomarf, whchi gmhit lowla oyu ot atienlmei htat e.iocch
aTht ai,sd it msese tomlsa libpeismso ot elur uot iwh(tout vyre eaitclhcn wdnlgkoee or seom idoepvrd eaemtprxinle d)ata taht the syhllitg larreg laeainn sedo otn piimar rdynhoge gnobnid eteenwb ongelcla meeolculs iva seictr ial)as(tp ererficeen.nt In leisrpm st,rme esinc naelain si e,alrrg yuo wlodu hntik ahtt ti sumt whmosoe iteernefr hiwt teh broegdoghinnd-ny atth orcusc thwi teh dpiyle-tw cylgeni.
---
ryilctt*S n,kesgiap ti’s nto teh bnmreu of ngydoersh but losa the retstnhg fo eht idelpo atht staeialcfti nogerydh odn:gibn a dynergoh obdnu ot a sgtnroly attireegeeovlnc oumlclee lkei ferinoul wlli ar“pep”a reom ipstivoe nad, su,ht no-obydnrgehd reom gtlnsyro twih a byarne gnexyo cor(dmpae iwth a oeryhndg neotcedcn to ,nocbra fro mpe.la)ex
erFhtru :nagdrei
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 ihtgm be ernogvikniht it ubt, H odnb minafrtoo of asa' msaek het aoeydcsnr currteuts fo eth roepnti (lgalnoec in ihts cs.e)a ehT Gyl ot Ala iuosttbtsuin deso sluret in sels H ndob ,taonfoirm utb of iniaudilvd asa' ont eewentb olcaglne moueleslc ht(ta mhtgi eb eomr ofr aynuertqra tusrt)urce
ryarimP rtectuurs = omnia adci ecnncSqdeosyu aeer ruusrcett = tuerusrtc ferodm itwh a inegsl naomi daic eneqsuec abe(t etaledp hetse, ahlap ,xhile ety)rrTtaiec ceuusrttr = ulemitlp coardsnye eurcststur genrinactti htetoerg utilelmp( baet epadlet ehesst kcatdse on opt fo aceh oreh,t tuna cryeer)tQar rrcttusue = peirton ettrsuucr erdfom from nfgldio of all taetyrri tursresuct ot akem bngndii s,iets et.c
neciS the naailen wsa put in caelp fo eht yenGicl, the imrrpya ruceturts asw belnua ot rfom na plaah lehix cnesi halpa exhil ersttrcusu ndee a rlrcpiatua queeensc (lyg - -x y) in redor ot orfm drhnegoy ondsb to ekep hte lhixe abe.stl
twha is ecgolaln ? a snrdcoeya rneotip turrset.uc
when you vormee egl,icyn hte smot nbudnaat nomia cida , fomr teh roerpscur luemlcoe illw uoy get a rprpoe ensrdacyo rteucsutr ? NO
yGl is lp,aor ieannAl is narponlo adn odhpc.oyhibr eMsseisn ovonsvetcnnerai otiamtu.n seThe AAs ahve etinferdf acmielhc rpeseroitp chihw dela to urdesdpti iterpon odglifn ace(dyorsn tre.utruc)s alSmiir ot Gul - lVa usutnbitsoit in elSkci lCle ees.Dasi
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$279$49I htnki it ahs soigmhnet to od twih cnyeigl eu(d ot tis asmll eisz ti nac ift in amyn aplsce ewhre hteor aonmi siacd acn nto dan echne ti rvpoesdi rtcuultsa“r atcsm”pnseoc to hte on,gcelal e..i ptu a nkki in teh halap xhl.)ie If lgeyinc is calipesdm yb gotnmheis l,ese I td’on tiknh gpolec-anlor acn mrfo tsi retcrco soyranecd et.rsutcur
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