I reduig,f g--XYnicely si ihcntlaleyc scoeddrein a “iaypmrr mniao dcia uetrcurts of a tpo”iern nsiec the ieftinondi fo a rPiamry eurrctuts of a reoiptn si a“ earnli haicn fo mnoai i.sa”cd fI oyu smse htwi hte myaPrri tecus,trur sa in eth toquines tsme, you oatncn rmfo het dryconeSa scrureutt of eht iporen,t wchih si rdeeidtnme yb the -idbdogonhnngery which rsuocc neewetb the edtipep cnkbbeao, nndneepetid of hte R gpruos. I eoph tihs adme sne.se
mroF iaedwipik: enoSc“yadr strucreut si rmfllayo dnedfei yb hte pttrnae of hdognrey sbodn eenbtew het maoni ygndrheo and blracyxo onxgey aotms in the pdipeet cbbnaoek.” pesms(hia enmi)
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 and i uotqe fmro e2r1/ttitgm.siwcmsisscdrsi0os:rleto//wecno4bee/apupoele.whattht/fpo-
9%"0 ehva an eiaitlnbifed eecting tanmutio LO
C A11 adn CLO 2A1
asescu
moraalbn nclolaeg r-gslcnsioikn avi a gniycel bintsutistuo in eth olgenalrpco uemclole "
whcih ansem that OI ash a cnlieyg tiibsuotnuts dan rehtoerf sit eblaun to fmor a anoredsyc rtustc.ureu
eDu to s'yncgile lamsl ze,si it rcaeets skikn"" in the monia dcia qces.enue ehTse ksnik rae dednee ot trclcyreo ormf the noysacedr srtercuut.
erOht ws:sraen
Y--lGXy si bnboecak rfo ocgaelln alhpa hi.anc 3 lncegloa haalp chnsai sprlia to rmof tpeirl lh.exi ynecGil hsa no R gu,rop alowlgin rof lbltxyifeii nda fonmraoit of eltpir ile.hx oN cgynile nevtesrp tihs cnsoutouin isrgpl,ian ipnvengert hte antfrimoo fo lcgoealn nerscoady rtetrcu.us
eRlcla hatt hsp-acaleeihl nad staeehtbse- aer aeepsxml of sedcrnyoa usctsterr.u iThs can eb gotuhht fo a itasnmietafno of eth laaph l.iexh
eAorhtN ayw to teg ta ti is vai eiliaoi:nnmt
.A dgohrney ingobnd wlnuotd aleyrl enaghc cesin hnereit aennali rno igcleyn are B.poral Gly t;g& lAa dhulo'tsn cghean ohw plnoeri is mofidide (I mnae ti CDULO, fi hrete saw a tsriec cnnirdahe or gste,iohnm tub not a graet rs Dn)awe. onnihgt ot ticiaend hatt cgnoalel godianteerd si erealdt in neeropss ot an AA .tunutsiitsob o,lAs ni the extotnc of OI (hwchi si the rnensegtip cpimlnat),o we dalraey nowk hatt eth eorplbm otdns'e ahve tnyhniga ot od tiwh eretnad,ogdi omer whit hte agchne in nc tf.trtEurucionseu/ synltoeH otd'n ko.wn
’Hseer neo yaw to -np-eeoscatfiseolmri scaree“edd bhoer-ynddnog ofo:”ainrmt mI’ ton a gbi anf of tish lnei of gaioersnn, tbu yhltnccieal ianaeln as a sedi uoprg hsa oerm gy*rdesohn ofr peoailntt hrygedon onnidgb ntha nicelgy:
lanane:i —3HC
yie:cgln H—
,So llenchi”t,cay“ inanela wldou piremt roem -nndeobrydogh mono,rfita cwhhi hitmg oallw you ot maitlneei ahtt heo.icc
tahT a,dsi it sesme asmtlo bmpssioile to ruel tou wthti(uo yvre laicctehn elngkedow or mseo ddoiperv mareeliptenx a)tad ttah eht hytligsl larerg nniaeal edos tno aiipmr ogydhenr dnobing eebewnt lolagcne oeuecsmll iva criets aplitsa() teirennercf.e nI lemirps e,smrt ncsei innlaae is g,alrre yuo luwdo ikthn htat ti smtu swoeomh eeniferrt hwti eth gnnge-biorhdonyd that sroucc htiw teh wleiydt-p ignecly.
---
Silrttcy* ,kpegsnia sit’ otn the ubrnme of rsgeynodh utb saol het tsrgtehn fo eth opdlie thta aeltfiacsit rnhdyoeg gdi:nonb a ndeygorh uodbn to a lotysngr taoretvlceeenig comlleeu elik lnuroefi lliw rpap“e”a orem toiiesvp ,dna uh,ts e-nynhbgdoord omre yrnlosgt htwi a bryane yngoxe rmcepdao( whti a gdnhryoe enccdteno ot croban, rfo xl)m.peae
Fhtuerr ra:gdine
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 mhgti be gnorvtikehni it btu, H dnbo oirtmnfao of 'aas askem the csanodyre uceusrrtt of het ertnpoi lo(ceangl ni thsi a)sec. Teh lyG ot Ala iittsnotuubs sode urelts in slse H donb omni,tfaro tub fo ddvalniiui aas' ont benewet cgnaello olsclueme a(tht ihgmt eb roem rof eyqrrtaanu tscretr)uu
ymairrP ucrsrtuet = miaon acid ceerecaeSsudn nqyo rtursetuc = reuttuscr defomr wiht a sgeinl noami adci qeceuesn a(teb daeeptl the,se alhpa xiel,h tieTey)r acrt ruucerstt = meptulil sycadeorn uutsrrscet tntrnaicieg egotrhet eiptlulm( atbe tdeeapl hssete ckdeast on pot of heac eto,hr r aurQrc)tnyeeat uetrcstur = nptorei ututsrrec roemfd ofrm nolfdgi of lal ytariert retstcuurs ot ekam bgninid ss,iet cet.
eciSn teh neainla wsa put in claep of teh Gcn,leiy hte maipyrr trsructue wsa nbalue ot form na aplha lxihe cenis lhpaa lxhei srutcuesrt need a irtprclaau uneeesqc (ylg - -x y) ni derro to fmor ordgnyeh sdnbo to keep eht helix ebas.tl
wath is cnaleogl ? a dscyraone iptreon etu.rucsrt
whne uyo movree ,nylcgei het mtso uanadtbn onmai cdai , rmfo eht osprrecur eeolclum lilw oyu teg a roprep andcrseoy tsreucrut ? NO
Gly si ,parol iAlanen is oanpnrlo and iypcorbhdoh. seMsisen eivononaectvnsr tmaunio.t heesT AAs veah fneietdfr chalciem ritseorepp chwhi alde to iestdurpd ernpito gdilnof odesnayc(r erstruu)tc. iimrlSa to ulG - lVa nsiistutubot in Sklcie elCl asise.De
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$279$49I kithn ti hsa hmostnegi ot do htwi ynilceg de(u to its mlsal size it nca ift in nyma clseap eehwr toehr anomi cadsi can otn dan hceen ti edrpoisv acrlr“usttu posc”enstmac to the loeanlgc, e.i. tup a kkin in het lapah .iehl)x fI gelniyc si limpedasc by hsintomeg es,el I o’dnt khtni ooplarlngec- nca ofmr ist rcetocr scyerdaon uuectr.rst
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