I dgie,urf c--ynlgYXie si ialenlyctch rddeesocin a rmryai“p aomin icad trurtcsue of a er”potin ncies the ftinndioei of a rimPary escurrtut of a ptorine is a“ linrea hiacn fo ianmo s”ac.di If ouy msse hitw eht arPirym ueu,trcrst as ni het tnuoqesi etsm, you onncta mrfo eth crSneoday utctrrseu of eht t,onierp hciwh is ieendtdrem by the n-boyerohdngding whihc cuscro eebnetw eth deetipp abkcoenb, enneetnddip of eth R ugrosp. I poeh siht edam see.ns
Frmo iadewkipi: arycdo“nSe crturtuse si omayfllr eddiefn yb the ptneatr of rgydnohe nbods ewteben het nmaoi heonyrgd dan lbcyoxra eygnxo matos ni het dppetei bcoaebkn”. eaisspm(h im)en
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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mlaorbna oecalgnl sniokl-srngci aiv a gcineyl utnbosisuitt ni teh rollngpcaeo uoemllec "
chhwi measn tath OI ahs a cglyeni stotsuubinit and rfteerho ist blnaeu ot omrf a sancrodye sruuctrtu.e
ueD to nlcye'igs allsm sz,ei ti eetcrsa ikk"s"n ni hte aomin dcai eeencusq. seThe iksnk rea nedede to rcetocrly fmro het srdnyaoce tue.scrrut
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reothNA way to gte at it si iva ioen:anmltii
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So, yneccl,“htla”i naealin lowud empitr eorm go-dbnhrnoedy marniooft, hwcih ighmt allow yuo ot eienmitla hatt checo.i
thaT ,asdi it sseem alosmt eplobmsiis ot relu uot w(iuhtto yrve litcnaech lgdkeewno or esmo pdreivod neelxtmpaier dta)a ttah eht lylgthis erlgra inleaan osde nto imripa hoygdren gbnndoi tebnewe alegocnl oceluseml iav eisrct a)(lsipat eencen.frtire In ispmelr rm,tse enisc ainaenl si ea,grrl oyu wuold knith ttha it tsmu oosemwh teneirref itwh eth nooebn-higdngrdy thta coscru whit teh yildw-tpe genycil.
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Sc*lytitr p,isagken it’s not het mrbneu of hodsgrnye tub oals hte enstghtr fo teh iepold htat atecstlifia ydnegorh bdnn:igo a hrodyneg obdnu ot a rogsnlyt reolveatnteegic moelcuel ekli refonuli liwl “p”rpaea omre eivtopis d,na ,tsuh benohnrgddoy- orme rgnoytls iwth a nbyrae nyxoge cm(aeprod tihw a dgryeohn notdccene ot ,caobrn fro ea.mexl)p
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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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ncSei eht naaneil swa utp ni alepc of eth ,eyGinlc the mrpyari sutertucr was uablen ot mofr na lapah hexli iscne aphal xheil uctrstseur ende a ctapaurril neesueqc l(yg - x- y) ni orred ot mfor ehdgonyr sbdon to peke teh xhlie bte.als
waht si elncloag ? a aordneycs piotern t.ruerstuc
nhwe oyu vrmeoe ,nylgeic eth tsom auntdanb maion iadc , mrof eht ruscroerp lumleoec illw you egt a epropr cnydreosa stcuerrtu ? NO
Gyl si pr,oal ielAann is noanlrop nad oiodcrhb.yhp nMsesesi noosnvitcareenv taoitnmu. seThe sAA ehva rentdifef ecilchma oetriseprp hwihc ldae to sitredpdu oprient nofglid ry(eoncasd cs.err)tutu iimarSl ot Gul - Val utibiusotnts ni ielkcS Clel De.iseas
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