I gerduif, cXg--iYleyn si cithnalcyel cndrdseeoi a ripar“ym anoim cadi stutrcure of a nrepoi”t ecisn hte oinenfdiit of a ryaPmir euctrtsru of a pointer si a“ rnaiel acnhi of noima isad”.c fI uoy ssme hiwt the Pyrrmai utetcsu,rr as ni eht suitenqo mtse, uoy catonn form the ecydaornS usrucettr of eht ti,peorn ihwch si eeddnmeitr yb the bgngohdrye-dionn hwcih ocusrc ewtbene eth edppiet enkbbaco, pndendietne fo teh R gsopr.u I pheo shti eamd e.nses
From daiipiwek: dcS“raynoe errstutuc si ylolarfm eeniddf by the ttnerpa fo oryhgned bsond beetnew eht aomni ynrhgdoe nda byxcrloa eyngox stoma in eth teppeid ebbacokn.” mps(eaish ien)m
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.
ok sguy dan i uqeto omfr .ttcw/hwpsrutc4eeimiwalsfohor-smot./s/etrs/aepl1tcso2i:dtne/pgeiboe0
%0"9 vahe na enfditeiblia ientegc iamoutnt
CLO 1A1 dan LCO 12A
asu
cse broalanm onlacegl kgnilcsnsiro- vai a cielygn ntiotusuisbt ni het grocoallnpe locuemel "
hhwci smena hatt IO sha a glciyen tsniuotsbtui dan thrreoef ist ubalne ot mfro a cedsyanor er.uutcrtus
euD to esngylic' lsalm zs,ie ti etreasc "sn"kki in the inmao cida unqse.eec esThe nkisk era nedede ot etoclrryc ofrm het dnscaroye .utrrsecut
eOhrt w:esnrsa
lG-XY-y is nebkacob orf eloangcl aaplh i.nhac 3 caleongl ahapl ishacn liprsa to ofmr eprtil hxeil. lneicyG sah no R ,rpguo nliogwal fro iiitelbxlyf adn rfntoioam of erltip exh.li No elncygi tsneepvr ihst sctuoounni pnil,riags ingtrepnev the tnroomaif of ocnagell rsdcoaeny trutrue.cs
clRela taht -aelpicahlehs nda aeebsehtts- era xmeeplas fo deocasnry eu.srtcrtsu hsTi anc eb gutothh of a oatanenisfmit fo eht hapla hexli.
rNAhteo ayw to teg ta it is aiv iaiinotn:eml
.A yoenhrgd dinngbo dlnwuto lyaerl nagceh csnei erhiten nnielaa ron iegyncl rea Bl pr.ao Gly t&g; lAa olsutndh' gcaenh who ineplro si dodmfiei I( aenm ti UOCLD, if heret swa a ctseir icnanderh or ihgtso,mne ubt ont a etrga )ra swn.De tihngno to iitceand hatt lncaeglo aogndeietrd si edatrel ni esoprens ot na AA .itstobtiusun osl,A in eth xetntco fo IO h(cwhi is hte tnsiegpner ,pma)tilcno ew ylraead kown taht eht blpeorm so'ntde evah nntaiyhg ot do hitw endaoie,dtrg rmeo thwi teh aecghn ni i/f.crotes Eutncnrutu oHstelyn 'dtno okw.n
reHe’s eon yaw ot conlis-seerfo-mpatei ecddra“see oh-nbdegydrno rt”fi:oanom ’mI tno a igb anf fo hist neil of e,oasrnngi tub lncleaicyht ilnaane sa a desi uropg hsa mroe sneoydghr* fro eaotnpilt oyrdengh dnbgnio tnah cginley:
nai:eanl —3HC
nge:ylic H—
So, la,“tecliyc”hn inalena luodw mritpe emor ohgnebrdn-ody ,arnomtoif hihwc hgimt oalwl uyo ot amieelint ttha c.ehico
taTh das,i ti smees asoltm opsbismile to lure uto (thoiwut yerv nclaihcet eldoekwgn ro semo eorpvdid eliexaretpnm data) that eht tsyigllh alergr aleainn edso ton ipairm yodnehgr nbngido eenbwet ncogella somlcluee aiv stcire pis)aatl( ince.eerfrent nI epmrlis r,esmt iescn neniaal si ealrgr, ouy lwudo nhitk hatt ti mtsu moowhse fetnreier iwth hte -ginhodgnneoyrdb atht cosrcu htiw hte pi-tdylew nligcey.
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iltyctS*r ,eisgkapn ’sit nto eht bmneru fo gosyndrhe tub asol teh hgetsnrt fo eht plodie ahtt isfciattael odhynrge obin:gnd a eyrdhong budon to a snortygl oeeagtclnireetv euloemcl liek lfiunore lliw pp“”reaa orme vpiotsie nda, tuh,s odryon-gdhbne reom rsgonytl hwti a ebryna oxegny peaom(rdc twih a ohgyrdne cnocetend ot obnr,ac orf ea.lpemx)
reFruht ngiead:r
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 htmgi eb ognrtiikvenh it but, H nobd iomaortfn of aa's maeks het adrenyocs strctureu fo the eptonir calngleo( ni iths a.c)se ehT Gly to aAl nubttisuisto deos elurst in slse H bnod tofra,omin utb fo ivnliiuadd 'asa tno beewten celognla cueloemsl at(th tghim eb mreo for yunareqrat r)eutrcust
yraiPmr esuctturr = miaon caid aqenc nudoSryeseec urtretusc = trsutcreu deform thwi a nilgse oanim idca ecesequn etab( petlead te,she hlaap helxi, trteTcyiera ) trtcesuru = uipmletl sodarncey rrttsusuec terganntici erethogt ltpliuem( aetb ldeapet esseht stdkeca no pot fo aehc heo,tr uectnrrt eayQr)a rrscutute = pnreito ertuctrus odefmr from oldgnif of lal teryriat esrttcuusr to aekm bngnidi ,isset e.tc
Since het nnielaa swa upt in lcape of het Glcniye, the ayrrpmi retcrustu wsa ealbun to omrf an halap xihle ensic palah xelih tcrsueutsr ende a alarrputci euecqsen gyl( - -x y) in drroe ot from rohgeydn snobd to ekpe eht xielh eabl.st
tawh is lnaolgec ? a dcenyoras ropient rc.etusrtu
whne oyu reomve l,icynge eth somt natndabu anmoi cadi , rofm the oscrrepur lcomeelu wlil uyo egt a repopr dscayonre tuetrsrcu ? ON
ylG si rp,alo Aileann si nopnarlo adn dhphibo.oryc einsesMs toicnnearvonves tam.niotu hTese AAs haev edfitnfer mecilhac eeistorprp hihwc ldea to ipsdrdteu ornteip figdnlo ocdsrean(y )ucerrttu.s rmiliSa ot Glu - Vla tutnsisoitbu in keiSlc ellC a.seeisD
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$279$49I kntih it hsa ioegmnsth to do wiht yiclgen (ued to its amlls isze it nca tfi in mayn cplaes erwhe horte aiomn idcas nac tno nad ceenh it dsoievpr ltcs“ruatru moce”sctpsan ot the elno,gcal i.e. upt a kikn in teh pahla exh)l.i If niegcyl is aepcidslm by nothseimg sle,e I d’otn thnik gpe-nlacrolo acn fmro its rrectco oeandsyrc rttuu.ecsr
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