I ,iefdurg gY-eyci-nlX si nathiellccy eceinrddos a “ripmary namoi acid ertscutru fo a ipeotnr” neics hte eiiiofdnnt fo a rPmairy tcurturse fo a npetrio is a“ aierln chian of ionam is”.dac If you essm htiw eth aiPrmry tucurtes,r sa in hte qnseouit esmt, you ntaocn ofmr teh Sednraoyc csreuurtt fo het ,ptnrieo hichw si ddniemtree by het bnghod-ngeonrydi ihcwh occrsu nbeweet het deitpep anbeobkc, eneddtpnien of het R p.grsou I hepo shti adme ness.e
Form iiekadipw: yncorde“aS suurcettr is yarmofll edfdein yb het prttnea of dnrheogy bonsd wbneeet the noaim ydehnogr adn orycbaxl xnygoe omast ni hte edtpepi eobknbca”. seapsihm( e)imn
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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chihw mnaes taht OI has a eiglcny ibssuittnout nda ehetrfor tsi nelabu to rfom a srdoeancy rtuust.ruec
uDe ot le'ngyics salml is,ez ti caerets ins""kk ni eth naimo iacd ees.enqcu Tseeh nkski ear eededn ot lectcoyrr romf het scryndeoa .ettrsucru
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calleR ttha shall-ieahcep nda btetee-shsa rae leepmasx fo nedracsoy t.rutucesrs iTsh cna eb ohughtt fo a itioaentfsamn of teh haalp .hliex
rNAeoth ywa to etg at ti is avi :ilentnmiaio
.A oerydnhg bigondn utdnwlo laryle geahnc cesni rtihnee nlaaeni onr cynelig rae .oBal pr Gyl > aAl do'ntshlu ecnhga owh orniepl is omefiidd (I enma it O,CDLU fi herte asw a streci eahcinndr ro si,omgthen but nto a gater ws. )earnD gnthino to ditinaec atht elaolncg idgoearnetd si deteral ni eornsspe to na AA .nttobsutusii l,sAo ni hte otcntex fo OI iwhhc( si eht nesienptgr pcimtln),ao we adreyal wonk that eht bmlepor no'tsde vahe nyniathg ot do ihwt dentdogi,are orme twih eth cehang in ctr/uurtoeusc.nEn tfi lntyeHos 'ndot nk.wo
re’Hse eon awy ot reetmnas-ieoosi-lcpf daes“eedcr hnydodnge-rbo :irt”ofmoan m’I ont a bgi anf of htis lien fo gonseir,an but cnaiehycllt ilannae sa a sdei rpguo ash mero dnshgyor*e for pnatlotie ednoyhgr dngoinb nath lyeincg:
nlniaa:e CH3—
ycige:nl H—
S,o ,clhl”tean“cyi lnienaa odwul eiptmr omre yh-ordnboedgn oan,fotimr ihchw hgmit lwaol oyu ot leitmniae htta ieco.hc
taTh s,iad ti messe msltoa iospmisebl ot eurl otu iwt(tuoh vrey lceaithnc okgedlewn ro emos pdrievod tmrlaeixpnee at)ad hatt hte isyhltlg gaerlr aalienn esod ton pamiir onghydre dongbin etenwbe laolecng eleouslcm avi ercist aap(s)lit e.cternfniree nI mesripl mr,ste sicen lnaiane si gerla,r uyo ldwou kinth htta it tsmu eoohmws efnrertei tiwh eht gednybornhgo-nid tath cscuor wthi teh deyw-plti leinycg.
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*Syiltrtc ne,apigks tis’ not hte enrbmu of ydeghorsn tub olsa teh shtengrt of hte ioedlp ahtt elsaiiatftc ydhnreog n:ibodgn a yrngdheo dounb to a tnslryog vegttieneerloac umelolec lkie ionreful wlli aepa”pr“ rmeo spvioite na,d h,sut noedhg-ordnyb omre yorstlgn hiwt a aryneb oxenyg pcea(rmod twih a rheoydng oeecdcntn ot bac,nor rfo .emapxel)
Fetrurh dn:girea
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).
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ewhn uyo evmero ygcni,el teh smot aatndubn ianmo cdai , romf eht soprrurce ollecmeu wlli ouy etg a perpor sndecrayo ucesrrtut ? ON
Gyl is aprl,o alinneA si onlrnpao and dbhhcioo.pyr esesisMn cennoteanirsvvo .mtinauto heseT AsA evha nifreetdf ichaclme eorpirtpes ihcwh aedl to siterddup tiernop oilnfdg sednycoar( c)rues.utrt miSlira ot Glu - laV ibitnotsuust ni ileckS lelC .eiDasse
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$279$49I hktni ti ash hsiongetm to od iwth lcgniey e(du ot tis asmll izse ti anc tif ni aynm spceal hwree ohret ainmo siacd acn tno and chnee it peodrsiv tt“cruslura cnoscmetas”p to the onaglel,c .ei. tpu a nikk in eht palha lxe).hi fI iglcyne is laimdpsce by gohesmnit slee, I on’td thkin gnrlleocpoa- anc mfro ist rceroct aydcerosn .ruecrtsut
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