I gerfu,id --ilnYcegXy is hncltiyaecl decrseodni a p“arrmiy naoim daic rrutectus of a ine”topr necsi teh foiiteinnd of a amrriPy erututsrc fo a peitorn si “a anilre hnaci fo noami .”scida fI uyo msse twih the Pamryir csretu,utr as ni the utoeisnq e,tsm oyu anotcn omrf eth eorcadnSy ettrrcuus fo het rieptn,o hiwch is irdmdeente yb het -rdbohgygidoennn hchwi uorcsc btnewee het teipedp koabecnb, pdeeitndnen of eth R o.urgsp I phoe ihst daem .essen
mroF diakepiiw: cy“ranSeod trtureucs si flloramy eendidf by teh epattnr of erydohng bsond eetwnbe het ioman hregynod nad aloycrbx oexygn mtsao ni the tiedppe conkeabb.” (sahmiesp mie)n
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 sugy dna i qeuot omrf brco/oh.wmsed-tes.t0tleecircswfps4wt/emoupogh2/ipoils/it1/t:stneaear
0"9% eavh an aftilniiebed cgeiten auimntot
CLO A11 nad CLO A21
sse
uac mroabaln ncogaell oiiclnrs-ksng iav a eligync ontsusittbui ni het rgealclnoop elemcolu "
hwhic emsan hatt OI sha a ngelyic utttnsboiisu and rtoheefr tsi elbanu ot mfor a esanrocdy .ucsruertut
eDu to nci'gesyl malls i,sez it esaecrt ki"ksn" in eht monai adic qce.enuse hTees nkksi ear deeden to lortcrcye mofr the ndescyaro .srcetrutu
retOh s:nwrsea
-yYGlX- si cbaenobk fro oneagllc ahpla iah.nc 3 ocglnela phlaa inhacs lrapis to fmro teplri h.lixe lneyiGc hsa on R prugo, wlolnaig rfo tiibexllfiy dna roitmanfo of ptrlei lh.iex No ncgilye pervtsne hsit nsuotuncoi nari,isgpl nveginetrp eht ntofiaomr of aoclnelg droaesncy utcreu.rst
Reacll htta ieschhapel-la adn eteste-asbh are meepxasl fo aecodnrsy curs.rutste siTh cna be httugho of a noamfsenttaii fo eth aplha exhi.l
ANrheot way ot egt ta it si iva ion:iilemant
A. rgodnehy godnibn dntowul lrlyea hcngea ceisn rniteeh alnanei nor igycnel are lB .oarp lyG ;tg& aAl t'lnuhdos ngeahc owh porneil is dioidfme (I mnea ti UCLOD, if ehrte swa a tciesr rnnicdeha ro ,ntosgemhi ubt ton a teagr wDn a)ers. ithongn to cdiaenti ttha llcangeo agernteidod si dlertae in oessernp ot an AA it.stnobtuuis lAos, in hte etxotcn of IO h(wich is eth nitenegsrp aonmitp,c)l ew dearaly nowk hatt eht pemblro 'doents ahve hniygtna to od htiw taregn,dodei emro hitw het chgnae ni trictEuunefs.urotcn/ Htyleson o'tnd .know
Hr’ees neo way to omnceirlei-oatpsfse- sedcdere“a o-dehbdonnyrg i:ofrtm”aon I’m otn a igb naf fo hist leni of ,aoirnegsn ubt cehliclatyn lniaena sa a side rupgo ahs mero eyh*gdrnos ofr eonltapit ohdgynre noindbg tanh gncylie:
aenna:li 3C—H
ylgen:ci H—
S,o ieclc“”yt,alhn nanliea dlwuo teprmi mero nobdreyohg-nd ratfo,inmo hcwhi ihgmt alowl you to mneatelii ttah cheoi.c
Ttha dsai, it esmse lomsta ibiosepslm ot reul uot hoi(wtut ervy tlcncaehi elnoekdgw or eoms vpeodrdi renxametpeil ad)ta ttah eth thlsgliy argerl naneali osed ton mipari ngeyohrd bndingo netwbee anloglec mceluloes via tiecrs )pati(sla rtiene.ceefrn In eprmlsi s,rtem nscie anialne si ,garelr ouy owldu thkin ttha ti tsum hemosow tfeeirenr wthi teh di-nonbyoghrnegd ttah croscu wtih the -wdyltipe glncyie.
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ltSt*rcyi skian,peg t’is nto het uemnrb fo dynrosehg but salo hte gnrhsett of the opledi hatt ictaflsitae ygrnohde bninogd: a ngyedroh dbuon ot a lsotnyrg lrotiveenecaegt olumelce lkie fuonrlie illw r”e“ppaa omre ieivtspo d,na t,uhs yhgrodbd-noen reom lngrysto itwh a neyarb noegyx aopm(redc htwi a ogrndeyh enotedcnc to abrnc,o rof mx)leepa.
hFrrute e:igndar
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 mihgt eb rnkoiietnhvg it ub,t H bodn fnoitroam of aas' maeks hte ancosyred rtecstruu of het epotnri cll(noage ni iths s.eca) heT yGl ot Ala stnsbitioutu sedo rlestu in lsse H ondb rio,faomtn utb fo niaiiuvldd aa's not wbneeet olncgela mecsleolu hatt( mhtig eb mero rfo tenrqayrua suuctter)r
rymirPa crrsetuut = inmoa acdi nncoaeqedeSrc esyu currsutte = ertcsuurt edomrf htwi a lnsgie inmao dcai qseenecu (abet dplatee ees,th hlapa x,lhei yercttareTi) tetrurusc = lpmluite deayncors rsctusuetr gniaerittcn hteegtro tll(eupim ebta aptleed teshes tcsaedk on tpo of aehc toreh, tecar)uyr etrnaQ tuctrsreu = intoerp tcrurteus edmorf mfro lionfdg fo lla raeytitr uruectstrs ot meak binnigd sei,ts e.ct
Scein teh naaienl asw tpu ni aecpl fo teh lcGne,iy teh prrymia utsuertrc asw uebnla ot mrof na ahlpa xheli inesc paalh iexhl rucstusret ende a iprulcrata eecuesqn y(lg - x- )y ni rreod to omfr ghrdeony dbosn to ekpe teh hixle ls.eatb
htwa si eaonllgc ? a yscderona eoritnp ut.usrcetr
whne yuo meorve cl,gieny hte mots nabuadtn manoi iadc , orfm eth srcerpuro loulecem iwll yuo etg a rprpeo saryncdoe tsercuutr ? NO
yGl si lraop, eAialnn is norpanlo nad rhoy.cpihdob enieMsss ctoriansnoveevn iantumto. esheT sAA heav tieffrdne hiclcmae oeprsritep cihwh edla to dtrseidpu renopti oinfdgl (crdayones ct)uu.trsre rSmaili ot uGl - aVl sstbitutunoi ni Sliekc lelC seDsa.ie
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