I feuidg,r cyXYl-gn-ei si elccithayln ceseridond a rprmiy“a niaom dcai ustterrcu of a nioper”t iencs het iiednftion fo a imrarPy rrstcueut of a pienort si a“ niaerl hniac of oanmi .dca”is If uyo essm htiw the miyraPr r,suutetcr as ni het tiusenoq s,met ouy nactno mrof hte ySncearod trurceust fo het roet,pin hcwih is dmreenedti yb het dnir-genydbgnhoo iwhch urscco beeenwt eht teieppd bebknaco, eedtnndenpi of het R osgr.up I eoph tsih mdae sese.n
ormF iadkiwpie: Src“edoyna urtscuter si amlylrof enidfde by teh etrtnap fo oynedhrg nsodb eeewtbn het ainmo nrhogdey dan xbrlyaoc enygxo astmo in eth pedipte oekabbnc”. saphi(esm 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.
ko gusy dna i oqtue rfmo utrm:eidt4tpglhewiofere/ensebtosi.aite1sc.wh/rm0op-so/csttowp/2lacs/
9"0% ehav na ilifneteadbi iecnetg itnomatu
CLO 1A1 nad CLO 12A
sa
secu maorlanb lclegaon s-cilkisronng avi a iglncye oitistubutsn ni hte glopcanelor mcleeolu "
iwhch anems atht OI sah a egyncil tsiitunsoubt dna therofre sit anuble to orfm a dyonaecrs scuutrue.rt
euD ot 'eygicnls smlla zise, ti tsecrea "iksk"n in teh maino cadi eqseen.cu ehsTe kiksn ear needed to cryetorcl mrof the roacnyesd rte.usuctr
ehrOt sra:nsew
l--GyXY is oenbcabk ofr gclolane lphaa ich.an 3 olneglac alahp snachi lraisp to fomr rtiple .xlhie nleGyci has on R ,pgruo glilawon rof ibflyitixel nad amoinotrf of peiltr xhlie. No ygcnile ntrspeve hits ctunouinso ,ilpgairns gnenepirtv hte oaomnfrti of egnocall yanedorsc ueut.rrcst
eacRll thta helahics-pael nda baeetthess- ear xpeelsma fo dcnsoreay tscesurur.t hTis can eb thutogh fo a nafosinmeaitt of het lphaa lhi.xe
eANhotr way to gte at it is iav nlia:tiomien
A. drgoenhy indobng ulonwdt rlylea gaehcn senic ehtnire aianlne nro lgeniyc are aop lr.B ylG ;gt& Aal nosutlhd' egcnah who rnpolei si imeodidf (I mnae it ULC,DO fi erhte swa a tiescr hncaerind ro nosigthe,m ubt nto a regat )w sr.nDae hnntgoi to dtciaeni atth cnloglae dodegrianet si atelred in seorensp to an AA ti.usbnotuits o,lsA ni eth txconte fo IO (cwhih si het npetrsgine nipmlto,)ac ew ylearda nokw that eht opmrebl eo'nsdt vahe yhnntgia ot do tihw ien,egaroddt omer htwi hte nghaec in cuEnnrs .c/ouurtfttei oyteHsnl d'not ok.wn
r’Hese neo ywa to ioeem-cnotfearls-pis dsdea“rcee grobdnyhno-ed onm”aorfit: ’Im tno a gbi fan of shit lnie of ,sgrnenaoi btu ctcihlylnae naniale sa a deis gourp sha mroe dh*gnseoyr for opettnial erdgnyoh nbgniod ntha cleigyn:
ni:alean C3H—
ilcnyeg: H—
,So cncay,litel”h“ aeailnn ulwdo piretm emro byoehgodrd-nn ifao,mtnor hiwch hgtmi allow you to melinetai taht cehco.i
aTht ,adsi ti meses tsamol bselpoiims ot rlue uto otuhiw(t yevr cnhetacli gdekewnol ro smeo ddevpori ilreetaxmnpe aatd) ttah hte lisltghy argrel lnaenai deos ont apiimr odeygrhn bgdnino newetbe aglconel smuclolee via ctirse t)ipl(asa r.erfeeenncti In pelimsr tsm,er eiscn naelnia is lrera,g you wdolu nktih thta ti utms msowhoe rreniefet whit eht hnoegi-dgdynborn ahtt sccour htwi the ltyedw-ip lycieng.
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*cStrilyt ksing,epa ’ist not hte nebrmu fo yheongrds tub aols hte gthenrts fo hte eldpio atth sitafclaiet gryhdoen ngdni:bo a eyhndrog bodun to a nyslgrot caetrteengvoiel umcoelle leik eirlounf wlli ra”p“eap reom tiesovpi a,dn t,uhs nhoydrd-gbneo remo gyontrsl htwi a eanybr ongyxe eodac(mpr thiw a ghdryone onncedetc ot bancor, fro axee)pml.
Fhurter gnra:eid
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 hitgm eb nkrvegitonih it ,tub H onbd noitaofmr of s'aa msaek teh dcynrsaeo seurrtuct fo het otreipn glao(nlce in hsti )a.sec heT Gyl to Aal usibitutsnot esod relsut in elss H nbdo ainomrfo,t utb fo andidliviu as'a nto eeenwbt lncegaol lecumsoel ta(th might eb moer orf raeuqrnyta uurs)ecttr
iarPrmy tusterruc = nmoai icda qennrecedyoacs ueS rectuurst = srrcteuut ferdmo tihw a lngsie oianm daci cneeeusq tae(b aledpte esth,e aalph lh,exi rcytTte) riea uutcerrts = lelmtuip rsneaocyd rcutsutrse naitetrcnig grhteoet (mletuipl tbea datelpe sshete asckedt on pto fo echa hoter, c ttQnaay)errreu teuctusrr = itpoenr uerscttru rofmed fmor ifdlong fo lla ariyttre ttuurrscse to kaem igndbin stsei, .cet
iecnS hte aanelin was utp ni elcap of eht inleGy,c the pyriarm trutsuerc asw lanube to ofrm an ahpal heixl ensic aalhp ilexh rsstruutec eedn a atriprlacu sqeenecu (ygl - x- )y in edror ot omfr odhgryen obsnd to ekep eth xelih s.tbela
hatw is gonallec ? a darscyeno reopnti ct.uteurrs
wehn oyu evemro gnl,ceyi teh otms abdnuatn mnoai icad , morf teh pursroerc umolecle lilw oyu tge a ppreor yreoscdan rusrteuct ? ON
Gyl si aor,pl nnAlaie is lornpaon dna .iydhbchroop ssseenMi avtscenvnnoiroe uoantmi.t eeTsh AsA vhea eendfirft hcamclie pprioreets ichhw aled ot diurpsted ptreino lfnigdo nredcyao(s uttsruce.)r raimiSl to uGl - aVl utinotsustbi in clkSie lelC easesD.i
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$279$49I hitkn ti hsa nhsgemoti ot do htiw ienyclg (ude to sit almsl esiz it nca tfi ni nmya lpeasc rehwe toreh nmiao iadcs can not nda enech ti odirevsp ruulttcasr“ ompc”sesatnc to eht oegnc,lal e..i tpu a nikk ni eht haapl h.xl)ei fI ilcygen is ecsdmlapi yb enhtimsgo ,eesl I ’ndot ihtkn aeoprcgoll-n cna morf ist croetcr neyradcso uuesrc.trt
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