I gdruei,f ng--ciXylYe si lelcyhintac sroieeddnc a apy“rrim manoi idac tcuustrre of a per”oint since the iinfietndo fo a riPaymr strrcetuu of a preonti is a“ irneal anich of nomia a.icds” fI oyu sesm hitw het ryaPrmi tcuu,serrt sa ni het iqtsneou tmes, uyo oanntc rfom eth rSdaoycen stutcurre of eth eroitp,n chhwi is emredniedt by the oibnnryd-edgonhg which csurco beneewt het pptedie cbanbeok, npeeednidtn of hte R .rupogs I hepo ihts edma s.seen
mFro iidwieakp: ydenarcS“o rcretstuu is lyorlmfa deeindf yb het atnpert of ydgohnre sndob ebenewt eth mnaio hrdnegoy adn baxrolcy nxegoy atsmo ni the ptpedie bnoaebkc.” e(sismaph nime)
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 yusg dna i uetqo romf m0ieco2theetracw/btrp/inp-:a/slr1ewefgoco.sseotil4ith.swposte//tdmsu
0%9" eahv na fenidtleiiba netigec tnoituma OLC
1A1 nad LOC 2A1
eas
cus lranobam lgeaocln iign-clnkosrs via a yelnicg uittbssniout ni eth cgnrloloaep clelemuo "
whhci semna htta IO ash a cneilyg sisutobtnuti and hereftro ist eluban ot omrf a ondaesycr tutrs.uuerc
Deu ot eynslgci' llasm s,eiz ti eaetrcs i"knsk" ni teh mnoia aicd es.qeucne hTees kinsk era denede ot erocytcrl mrof eht srcdeonay rusetcru.t
ertOh :aserwns
-GYXyl- is eabcnokb ofr alongcle lapha i.nhac 3 eacgnoll lapha anhsci alipsr ot mfor lrtiep iexlh. lGyenic sha no R grp,uo ilalwgon rfo lytiibifxel nad noriomfat fo itpelr h.xiel No nlyicge nprseetv tihs stuocounin sanprli,ig ivnternpeg het foimranto of laolcneg doansercy rsctr.uute
caRell hatt slaele-pchiha dan seseteabt-h ear amspelxe of cnasrydoe .setucrturs ihTs nca be ttuhhgo of a iianfamsteton fo the laaph xi.lhe
AehNotr ayw ot gte ta ti is vai niitm:neaoli
A. egyndohr niongbd uodtnlw arleyl nacehg scnie nirethe iealnna rno gienlcy rae a.lpBro yGl &g;t aAl tnduslho' achneg woh npelroi si omdfieid (I anem it LCUO,D fi ehetr saw a stceri achnrdein or oihtsmn,ge btu ton a gaert D rn.wsae) onnihtg ot ciendtai hatt oglanlec toerdgained si erldtea ni pesnesro ot na AA .btsoiusutitn As,ol ni teh ontctex of IO whchi( si teh ngrteenisp ,oncpi)amlt we areadyl kwno atht eth lpeobmr ndt'oes hvae hgiyntna to od twih ngadieeodr,t emro iwht eth nhagec ni s itt/.nurntoerfccuEu nHstoely od'nt n.kwo
esH’re eon awy ot crsmeepa-tilnosioe-f cdase“dere dngyedbhonor- ofm”otanr:i mI’ nto a gbi naf fo shti inle of aerongins, tub nachycieltl ienlnaa as a deis gurop sha emro gnrsd*oyeh ofr tienaltpo oenryhdg odnibgn athn gnelicy:
:ealnina —HC3
cnyel:ig H—
So, cca,“hiylle”tn lnainae olwud mptrei oemr b-goonrdedhyn i,antrfomo chwhi thmig wlola yuo to mitelenia htta ec.hoic
htTa ads,i ti sesme stamol oilbesspmi to leur out htw(iuto reyv cicnatleh egondelwk ro msoe dovdrepi eairxetlnpem da)ta tath eth llsyhtgi rreagl neaailn deso ton miaipr dhyegorn nginodb wtbneee llancoge oemescllu aiv eitsrc tila)(psa ifrnnecretee. In sierlpm e,trsm sncie nalnaei si err,agl oyu wdulo inhtk atht ti sumt whomoes ertfriene tihw the rnhd-digyeonngbo atht srcocu htiw hte -ydtipwel elcigny.
---
ryt*lScti an,ipsgek s’it otn eht remnbu of odygnehsr btu saol het nhgtetrs of het leodip ttha leacstiaift hyedngro ndn:obig a dyghonre buond to a solrytgn toaelregetcievn cemuolel klei ieflorun illw raaep”“p omre vietiosp nda, u,tsh eryobnhd-nogd rmeo ystlorng ihwt a nybaer yexnog copme(dra wthi a nrgodhye eccnodtne ot c,anobr ofr eep)xm.al
uerFtrh greiad:n
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 thimg eb inigotnvehrk it bu,t H donb fnomrtioa fo 'aas emksa eht daysencro usrtetucr fo eth tpeinro eolalng(c in shit .aec)s hTe lGy ot alA tsniutbuosit sode rsutle ni slse H donb aoitronfm, utb of aidnidluiv 'aas not eetenwb anlogecl eucmsleol tht(a gmhit be mroe for yquaerrnta scrruu)tet
mryaPir rtctusreu = miona icda ec rnSsaeqocnyueed errttuscu = rtceusutr erodfm with a lsegni onima cdai sueqecen e(tba dtpeale e,esth lahap xeh,il r)eetTyctrai rtesurctu = eplmuilt socenrday rttrueucss engitcartni gheortet tilp(umel etba pedlaet stsehe tsckeda on pot of cahe ,hrteo trntaQr rceua)ey cutesturr = iopnrte surrctetu dmefor frmo nlgfiod fo all rytaitre truercstus to kaem ignndbi seits, ect.
incSe eht innelaa was utp in cpela of eth el,Gcniy hte rmaypir stetrrcuu aws nbuael ot ofmr an phala ielhx ecsin alhap ihxle tucretsusr dnee a paliuarcrt qeeseucn gyl( - x- )y in eodrr ot ofrm ryneoghd dsnbo to kepe hte lixeh elbta.s
athw si gaoelcnl ? a dynascore rioeptn srertcu.tu
wehn ouy merove icngley, het tmso nubtdana omian daic , omrf het cuerprosr uecmlelo wlli uyo tge a epporr roeayscnd rstruceut ? NO
ylG is alr,po Aainnel is ooprannl adn ohhyibrdp.oc inesMsse rtoevsacnnoeniv tino.autm esehT sAA have rneefftid lhcacmei eerppositr hwhic edla to rptsueidd teionpr fnogidl sno(yrcaed )rtecrt.uus liirSma to uGl - lVa otnstiuubtis in Sieckl lCle es.iDsae
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$279$49I hinkt it sah isonmegth ot do twih clgniey u(ed ot its almls zise ti can tfi in mayn eslpca rehew orteh moain asdic acn ont dna ncehe ti vieosrpd “tutrrcusal sema”osntcpc ot hte nlcael,go ..ie upt a nkki ni the apalh eix.h)l If lngceyi si madsicepl yb eontmhsig el,se I td’no ihtnk ol-lrenopgca acn romf tsi ercorct srodyneac ururecs.tt
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