I ,feigudr -n-cyleXigY si eanlhcltcyi eddnercios a pa“rimry monai idca tesurrcut fo a ”reptnoi ecnsi eth odiiietnfn of a Pyrmiar retucsurt of a nitpeor si a“ anleri hanic fo iomna dsca.i” fI you essm thwi eth Prmrayi uutrrets,c as in the unqtoesi met,s ouy natonc ofmr het eonySracd stucrtuer of het ,tonierp whchi si ieetreddnm yb the rbgenygodihdn-on chiwh orsccu nbewtee the eptpied cokbnbea, dneeipdtnne of the R rspo.ug I phoe htsi adem nses.e
ormF aiidpiekw: dyrc“enoaS ctteusrur is larylmof nideefd yb eth arepntt fo yrgheond bsndo enweebt the monia ohgyedrn and xoclrbya xgeyno amots in het dppitee bobnckae.” ihem(pass )niem
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 gsuy dan i uqote fmor lmh/wt-ecogisopd0s/etotam.eci/ts:1lebwarrtse/oent2fi/4eocpshtpurwsi.
"09% ehva na ifeadtnilieb cetgein oanmttui LC
O A11 nad LOC A12
scaeu
s nolbrmaa nglcleao inlskirocg-ns vai a gicnely osbsittniuut ni hte plragcoolne clomeeul "
wchih nemsa that OI hsa a eigcnyl sbtinisututo adn orehreft sti lubane ot ofrm a acyerdnos c.eturtuusr
euD to siygncle' lalsm ,zeis ti ecersat kik"ns" ni hte niaom aicd encsq.eue sTeeh ksnki are neeedd to crryltceo omfr hte sndeorcay rrt.tcusue
htrOe rnasew:s
-lGXY-y si ebokbanc rof oglencla plaah ain.hc 3 loancegl aaplh hasnci lisarp to rfom rtilep xhe.il ilGycne sah on R ruo,gp naogliwl for iyfitelblix nad fonmtiora fo tieplr elih.x No cegnily rtevesnp htsi tioucsunno p,gnirlais tgvieerpnn eht nfotoimra fo oleglnca dsonrycea turestur.c
Ralelc htat ahlsch-liaeep dna sb-ateeseht era emsapxel of cesonrady s.cuuttersr ihTs cna eb hhttuog of a ttioimfaesnna of eth laaph eihlx.
NAorhte way ot teg at ti si avi imientianl:o
A. hyroendg donnbig uwnltod ellayr anhecg necis itenhre iennala rno eyngicl era lparoB . ylG t&;g laA lnt'dhous ncegha how eprnilo si ofimided I( eamn ti ,OLDCU if terhe saw a irscte idehacrnn or nimgt,eosh tub not a regta nw.Das )re ntinohg ot itndieac ahtt aclolgne idneotderga si traeedl in nresesop to an AA uuttssobin.ti ,olAs in eht ottcenx fo OI ch(hwi si het ntsrepegin l),mcopnait ew delayra nowk tath het bleprmo snode't ahev ihnagytn to od ithw otrd,gineade moer whti the agechn in ciuur./tufen totrsEcn ltHensoy ton'd nw.ok
sHe’re eno ayw ot splin--soaeeirmefcto ca“deeesrd ygobedornndh- raointf:om” ’Im ton a bgi anf of thsi nlie fo genainors, ubt italyclchne naaenil sa a ides urgpo ash erom sr*ygehdon for ttelipona hgyrendo indobng naht lgeycin:
:enlaian C3—H
nce:igly H—
,So ”hnct,“ciaylel nelaina uwlod mirept eorm ohbgrdeyo-ndn onrimfa,to hhwci hmigt olalw ouy ot tenielaim atth ciehc.o
athT ds,ia ti sesme oamslt seolpsbiim ot uerl tou uwtohi(t very naclthiec dwolkeneg or oems vperdido exmranipeetl dt)aa thta hte shltygli glrera lnaaine osed not aimipr gnedrhyo bnodgni etnbwee lgaconel esluoemlc iva escrti as(lp)ati necrietfene.r nI merlpis mest,r iscne niaanle si aleg,rr ouy dlwuo thnki hatt ti tsum hmsoweo fieetrner iwht teh rnbiohonngddyg-e ttha crsocu thiw eht ie-pytwdl ceynigl.
---
c*tyiltSr aigeksn,p tis’ nto hte eubnmr fo dyoesghnr but olas hte testrhgn of teh diepol ttah alfctiietsa yhognerd ndo:gnib a ynhrdego udonb to a oystgrln egeteclirvenota lmuloeec lkei eoiufnlr illw prp”a“ae oemr eivpstio and, ,usht ydonrdghnobe- erom rngtlsyo tihw a erynab gnyexo adomecp(r hitw a yngohrde nndcectoe to rbcano, ofr xeae).lpm
Fteruhr :anregid
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 ghmti be ongehvrintik ti b,tu H dnob ioanmtfro of as'a sekam hte edsycraon rutcsuert of het enrtpio (lagonlec ni tsih a)esc. The lGy to aAl butountissit oeds tlsure ni sles H nodb rtafno,imo but fo lundivdiia 'asa tno ebneewt llcgenao oslucmlee (that mhigt eb oemr rfo enaqutyrar rtec)rsutu
rPamyir cerrtuust = nmioa idac dyneescqaroee ncuS usurcetrt = rteruutsc omderf hwti a sngeli aomin adic eqesnecu eatb( patdeel eh,ste hplaa eix,lh ei) tacertrTy uuersrtct = pitllemu ynacdesor sseurutcrt eitcinrnagt getthoer lemtip(lu eatb ldpeaet teshse easctkd on opt of hcea r,heto eyQanurt)et arrc tuutrresc = eioprtn rerstuuct reodfm mofr dgilonf of all reryttia tuctursesr to maek nndbgii iet,ss e.ct
neSic eht nlinaea was put ni ecalp of the ,inceGly teh amirpry cturreust asw ebluna to ofmr an apalh elhxi iencs aalph eihxl resusttcru need a cilrtparau sceeeuqn (lgy - x- )y ni rrdoe ot mrfo dgyneohr dbosn ot kepe hte xehil atlb.es
ahwt si gceoalln ? a casoydrne pniorte trcut.uers
hnwe yuo vrmeeo ielyg,nc the most badntuan omian cdai , rfom eth scerrpuor ellcmoue illw yuo etg a pepror nardecsyo etrtcuusr ? NO
Gyl si olpr,a Aanelni si onprolan adn odyo.bpchrih eesisnsM vnsoeorantncevi imton.atu eTshe sAA evah rfneedfit elmcachi rpetiorpse hiwch eadl ot rdispduet eoiptnr lofnigd yr(cedsnao e.r)curtust malirSi ot lGu - laV oitusnstiubt in eSlkic lCel ies.seDa
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$279$49I hintk ti ahs mhnoitegs to do wiht ycingle due( to tsi llmas szie ti anc ift ni nmay pcelsa eehrw rohte mioan casdi cna otn dan ehcen it ispvdroe tr“tuslrauc ecnsmoaspt”c to eth negolca,l .e.i put a ikkn in het ahpal eilx.h) fI lyeicgn is adescilmp yb igetmhnso eesl, I dn’to hnitk co-onrglplae nca mfor tsi crctero dnyosacre sreut.cutr
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