I gd,urief --XilecgnyY
is hylcanecilt oidderscen a rpry“iam manoi cadi treruustc fo a troneip” inesc eht ndeitiniof fo a rPmirya esucrutrt of a reopnit is “a erainl hcina of noiam si.acd” If oyu mess thiw teh aPirrym urertt,ucs as ni eht onseutiq emst, oyu anntoc ofmr the dSreocayn rutceutsr fo the ,pronite iwchh si eidetrdmen yb teh -ghorninbengyddo ichwh corusc ewetnbe eth epdeipt knobebac, needtndepin fo teh R rpos.ug I ohep tihs adme en.sse
mFro aidepiwki: d“ocenSyar csuetutrr is laymrlof fdndiee by het rttnepa of rohdngye ndsob tewneeb eth namio drheynog adn lxbacory ngxeyo omtsa in het ptdpeie ocbabenk.” (aeshsmpi m)nie
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 sgyu dan i utqeo morf saponh/i/es/tor0oth2r1ms/c:betpaelge4ustctfiplctre/iww-toem.dis.oswe
%90" ehav an idliaefeitnb ietegnc iuotnamt OCL
A11 nda OCL A12
secau
s bnlraaom gneolalc nsoisk-gnlirc aiv a egilcyn tbtnisuusiot in the elngoaorlpc mueleloc "
hhicw aenms ttah IO has a iclgney tuiotbutsnsi nda foehertr sit bnleua ot morf a eosnydarc uusrtue.crt
ueD to iynleg'sc lsaml ,siez it esraect n""kiks in eth moian idac .ncqeuees esehT snikk ear eddnee ot rtcrecylo rofm het dscraonye rut.rscteu
hterO sraw:sne
XyG--lY is ecbbonak fro cgleonal aalhp ai.chn 3 oclelagn laaph nsiach saiprl to omfr ltreip xl.ieh lyeGcin has on R orpgu, noaillgw rof bliifletyxi dna ntrfomaio fo lieptr e.hixl oN lcngiey sprtvene tish sonniucuot aisginrl,p etirnnvepg the fniotroma of leacolng nedosayrc .rtruescut
cRleal hatt heaasclephil- dan eshsaee-btt aer maxplese of eoadcysrn su.sttrceur hsiT anc be tuhtgoh of a natnesoaitmif of the phala xei.lh
hNetrAo yaw ot tge at it si iva aoe:iintnmli
A. dhyrnoge gdnonbi tdownlu lerlya hcegna icesn reethin aiaenln ron ycnglei aer poBl a.r lGy g&;t laA tlud'hsno anegch who nileorp si domifedi I( amne ti ,ULOCD fi ehret aws a cstrie hnanrdcei or shgeino,mt ubt ont a agrte a r)wnDs.e gthonni ot iatdenic htta lncaegol eetdirangdo si rtalede ni pnreoess to an AA nssiuttuobi.t ,lAso ni hte cxeottn fo IO hic(wh is eth rgnesiptne )timcalnpo, we aelyadr nwko taht het omlrpbe dten'os aevh gnyntaih to do hitw inegd,rtaoed eomr hwit het gneach in /ouc.ut srinrutfcEnte yenHtols 'ntod nwo.k
seH’er noe ywa to mfopi--neetosciearls “racdeseed -hynbdegodorn ”rfamnio:ot Im’ otn a igb fan fo tshi elni of nigears,no tbu lnahleytcic ianealn
sa a side rpugo has meor sdye*gnhro rfo toeaniptl oynrhdge nnidgbo ahtn encigyl
:
inanae:l
—3HC
icyngel:
—H
oS, hctycl“ielan,” aneilna
wdolu miretp orme dob-eodrngynh a,omiorftn which itmhg owall uyo ot etelnamii that ccohe.i
htaT d,asi ti mssee smtola iomislbpse ot urel uot t(woituh reyv icnhtleac weegndkol or esmo irdedpov ixelpmenreta data) hatt teh lhysitlg garelr elanani
dseo not miirpa ndygehro ndgonib twebeen colnaegl slelcuoem vai cister s)aplat(i tneceirnef.re In lsirmep ,tsemr sneci ilneaan
si ,grrlea you dwoul itknh atht it mtsu weomhso ifnerrtee htwi hte ynoebhdogir-dgnn htat cucsro thiw the tiwpdl-ey inlgecy
.
---
r*ltSicty gnsepaik, ’its otn hte unmbre fo ysrgenhdo tbu laso teh htngerst of hte odplei tath tlciafaties oeyndghr gio:nnbd a dhnogery bdoun to a lyortgsn oveigerletecnat ucelleom klei leruonif will ar“a”ppe oerm eiispvto and, t,ush yne-oohngbrdd mreo srntoygl wthi a braeyn gxonye ao(dpecrm hwti a hdynrego ndncctoee ot ,ranobc ofr mxael)ep.
htFrure ar:dgnie
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 gmiht be rvokngithnei ti ub,t H nbod omafinotr fo asa' kemsa hte nascyredo rcustruet fo eth ipoernt coglnle(a ni this e)cas. hTe ylG ot aAl ibuonuisttts sedo rselut ni essl H dobn ooi,rnfatm but of dliidivnau asa' nto ebtenwe ecnlgoal leuecomls t(hta ighmt be mreo ofr autyraenrq e)ructtrus
Parryim erutusrct = amoni dica oceSedencrue qasyn trurcutes = tursteruc rofdme whit a esngli ioanm dcai eeuescnq ae(tb leedatp hseet, apalh ,ixlhe etrieTrtc)ay rctturuse = puemlitl sdaycenro srttusceur enntcraigti rhotegte eiu(llptm etab daeetpl ssethe csdtake no top of hace ht,ero atnruaec) eQrrty rutecstur = nietrop uursrttce mrodef mofr idnlfog fo lal terratyi stsutrrecu to ekam gibnnid tis,es ct.e
ieSnc het aeainln aws utp in capel of het nlyGc,ei teh rmraiyp uetrtrsuc saw nuleba to ormf an pahla ihlex iensc hapal ihexl rtsrucuest eend a rrtalaupic qceunese (lyg - -x )y ni rreod ot omfr negrdoyh ondsb to peke the lxihe satbl.e
tahw si llcgaoen ? a yosranedc toepinr etrrus.uct
enhw yuo roemev cgnylei, hte sotm uaadtnbn oniam daic , ofrm teh erupsrrco olueemlc lilw you etg a prpore cyearsndo tuersrcut ? ON
yGl is lapro, eaAinln is oplrnnoa and hrcphibooyd. esssniMe rvnaveoonceints timatonu. eeThs sAA ehav nefftdrei almchice srrpopeiet whchi dlea ot drtsiepud rpioten gfilndo ncy(esoard euuct.)rtsr amSirli ot Gul - Val iossuutbintt in liekcS Clel .esaiDse
submitted by ∗wasabilateral(47)
It can be re-accessed by making a purchase.
Purchase your membership here
$279$49 65% OFFI khitn ti has nhoietmsg ot do ihtw ilgceyn (edu ot tis lmsal isez it acn tif ni yanm speacl ehewr trheo minoa dscia anc not nad hncee it oversdpi sctutal“rur scte”paocmns ot teh ol,lcange ..ei utp a kkni ni eth ahpal el)hx.i If icgnlye si pedlsmaic by stonghiem ese,l I n’otd ntikh orploleagnc- can romf ist erccrot ernsaoydc rrsutuetc.
$279$49 65% OFF