I uerigdf, -YyngeliXc- si hletailcync rdidoneecs a iyrp“rma noima daci rtceusrut of a itn”rpeo inecs teh eiitoindfn of a yaiPrrm truesrutc fo a eiorntp is a“ ainrle cnhia of amoin ds.ac”i If yuo ssme whti eth Prmyari tecusru,rt sa in hte snoeiqut ,semt yuo ntnaco mrof hte rycnoaeSd urusrctet of the piotrne, cwihh si iremendtde by het gnnendgro-hbyiod hwhic rscuco eeewtbn teh tepepid obabncek, tenipdendne of the R gus.pro I epho isht made esns.e
mFro apiwidiek: “noSrcdeay cttsrureu si rlmfyola ededinf yb hte apttenr of egdohryn nsbod neteebw the maion negryodh dan loracyxb oexygn amsto ni teh etdppei obcnekba”. sme(apshi im)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.
ko yugs adn i oqute mofr -tmttn.o/tei1sieo.eid/pe2:gw0t/prrccewhhuwalfacssoostrt/sopism4b/ele
"%90 ehva an dlabeitenifi ceeignt unttomai C
LO 11A nda COL A12
uc
essa oalrbnma gollnace -ssoilnnkrgci vai a gnciley tutinbtiouss ni teh oelnalgpocr leuomlce "
hiwch mneas tath OI hsa a niyeclg nuisoutsitbt dan trohrfee tsi ualbne to mrfo a carsdeony cuu.strrute
eDu to gicn'lyes amlls s,zie ti rsceeta kin""sk in teh maoin adci seq.enceu Thsee ksikn era dndeee ot rcrolyetc fomr the onseryadc rrutes.tcu
tOher naew:ssr
YlyX-G- si oenkacbb rof elclgoan halap niac.h 3 cegnlloa alaph ainshc ilarsp ot ofrm tlrpie lhx.ie nleGcyi has on R g,rupo oallwgni orf yltiixifbel nda imtfoorna fo eirtlp .lhxei oN nlgecyi estevnrp tish cnisonotuu igirpl,nas erptinvgne hte aniomfort of necolgla rodneaysc resutu.crt
lclRea tath chaih-eellpas dan eb-stseehat aer mxlesaep fo nyoesrdac stsutcu.rer isTh cna eb htoguth fo a fntaastnimoei of the hlapa .ielhx
ehAtNor ayw to teg ta ti is vai itinlanio:em
.A ognerhyd bngdion tlowndu ylrela hcgnea since etinhre enanila nro cgelyin rea .pBr lao Gly &g;t alA hd'slnuto cehnag woh niporle si dimediof I( mnea it UCOL,D if erhte swa a rteics rdneicahn or t,isoenmgh tbu ton a gerta s).aw Denr ongihtn ot neaitcid that oellcnag degtreonaid si tdeaerl ni psrnoese ot an AA .isitstbnoutu Als,o in hte tnecoxt of IO hcw(ih si het respnetgni ia)ptmc,nol ew ayldear wnko ttha eht poelrbm 'sdenot veha tnyianhg ot od twih oidrgedant,e omre wthi het hncgea ni su.tcerr/oE uiunttcnf lnsoetyH dton' nk.ow
’erHse noe wya ot crolaoepesfsiin-mte- ec“redasde -odngyeobrhnd moift”n:rao I’m ont a ibg anf of sith ienl of n,nrgoiase utb hecnycaillt niaalne as a seid porug sha mero ygoehsrd*n rfo ittlopane ghydoren gondbni hnta igcneyl:
niaa:nle H3C—
c:igleyn H—
S,o ic”lyn“tahe,cl nniaeal lduow tmreip omer ooden-rbngdyh mntoafroi, hwcih higmt laolw yuo ot nmetlieia that .coechi
thTa sadi, it smsee tmosla ispbseiolm ot urel otu uw(tohit eyvr cahectlin koldnweeg or omes vodeprid xemteealrinp dt)aa ttha het siyhlglt elrrga iaanlne edos ton mraiip dnorehyg nobdgni etnbwee ogacenll elcleousm iva crseit la(tpsai) ertefcerne.in nI lrepism s,emtr ensci aneianl si r,arleg uoy wodul hntki that ti mstu oewsmho nrrefieet hwit eth oeognyndhngbdi-r thta sccour hitw eth id-lyeptw cgeynil.
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tStric*yl ,kesapngi t’si tno hte burenm of nysodrehg tbu losa eht tengrhts of eth dlpoie tath attifacelis gdyhreon dgnnbio: a oenygdrh undbo ot a tgrlsony itetorecglenvea ucloemle ilek loenurif wlil pr“a”pae moer iviteosp ,and ht,us hdn-gobnoyerd reom tlsgroyn ihtw a enyarb neyxog rpeod(acm twhi a grdhynoe dnccteeon ot cranob, for x.)peeaml
etruFrh di:ernag
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 gthim be vkirioetnhng ti ,ubt H nobd ifmtnaoro of saa' emask teh neacorysd etstruucr of het inerotp gnela(clo in shit ce.a)s Teh lGy to Ala suttubniiots does uelsrt ni lsse H bodn omafintr,o utb fo lidnivuida 'asa ont ewtnbee olleagnc uoelmlces (atth mithg eb moer rof yqaanrteru uectsrrtu)
riaPmry ttescurru = aoinm daci sc Suyoenedcernqea utsucertr = uutcrtsre mdfroe wiht a neigsl oanim daic ceuseqne ab(et deetpal es,eht aalhp he,ixl )cartr eiyeTt turtesruc = tmillpue ryodsanec usrrcuetst tirntneicag rtgtheoe i(mpullet teab aletdep seesth dkcteas no opt of chae toe,rh yetar cQaurert)n trtsruuce = inotper eurttusrc fmeord orfm niflogd of lal trtreaiy rucuertsst to eakm bdignni ,eitss cte.
nieSc the alianen was utp ni pcela fo teh nc,eGiyl the ypairmr stcrrtuue swa unleba to mfor an hlaap ixlhe inces lahap ixleh rurtuecsts eden a rriutlapca equeecsn (ygl - -x )y ni rrdoe to form onyegrhd odbns to peek het ielxh teblas.
thwa si cagonell ? a ndrsecyoa pternio .rteucturs
ehnw ouy mevoer y,nilgce teh tsmo daantbun moain iacd , rofm eth rcrropuse elmleuco will uoy gte a rpeorp scydreaon ttrrcesuu ? ON
lGy si la,orp ilaenAn si plaoonrn and pirodbo.chhy ienMsses oocnvavietrnesn aui.mottn Tehse sAA aveh edtnieffr aiceclhm irperptoes ihwch dela to diesudrpt repinot fdonlig csy(eoadrn uc)r.surtet amrilSi to Gul - laV ibstutiutnos ni icSlek elCl ssai.eDe
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$279$49I kthni ti hsa osihetnmg to od ihwt elyginc d(ue to sit mlsal eszi it cna tif ni ynma psecla erhwe rhtoe mnioa daics acn otn dan cenhe ti rievpdos tctrul“ausr tpsnmsa”ccoe to het a,lnclego e..i ptu a nkki ni teh plaha e)xh.il If cgnilye is cpdilaesm by tmsohegin seel, I ’ndto ikthn lpoolcreagn- cna mfro sti crtcroe anyscedor ecrttusur.
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