I df,eugri ilygn-cY-Xe
si chtenyaclil ienrdedsco a rpri“mya oaimn aicd uurstterc of a piote”nr necis hte fntidieoin of a yPmairr eucursrtt fo a tiopenr si “a lairne hcian of noami .sda”ci If uoy smse whti teh mraiyrP ,ucteusrtr as ni teh nsteuioq smte, you aonnct morf eht ceoySandr rtuurctse of eht e,tponir cihwh is eienddtmre yb het gdhordebgyninno- hicwh ocrscu teeewnb teh epditpe nbkcaoeb, nndeedintep of eht R opurgs. I epho hsti dmea nse.es
morF kwiipadie: do“ancyeSr tesuurtrc is mlaroyfl deeindf by the eattrpn of egyohdnr sodnb enetweb the amoni eondhgry and borycaxl xnoeyg staom ni eht ipteedp ekonbcab”. pamhe(iss nmie)
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 gsyu dan i quteo rofm ipt.rw/et//ech1tistocs/./e4imeewsowpulralr2n:sds0tof-tgtcsemeopoiahb
"%09 evha na niibaietefdl ieegtnc mtniotua OLC
A11 dna LCO A21
seausc
mablrnoa celgnlao s-liosnirckng via a gnelyic ntbiustoitus ni the ploengraocl oelecmlu "
hwich emsna ttha IO sha a neylcgi tbsontstuiiu nad otfrreeh ist lnuaeb to rmfo a sraceyond ue.strcurut
eDu to ns'icglye lsaml z,ise it atsecer is""nkk ni eht ioman diac euqse.cne sThee skkni rae eeendd ot tcolerrcy mrfo eth onecyadrs seutrt.cru
htOre sasrwn:e
X-G-Yly is naobcekb for oencllga aaplh niahc. 3 aelnogcl palha nchasi slprai ot fomr tlerpi e.ixlh nycGlei hsa on R up,rog nwlglaoi rof fybxliitlie nad minrofato fo elptri hxl.ei oN lngcyei tesvpnre thsi uintcusoon gilrn,pisa vnetnripge het mfoainrto fo onclgela nsydeaorc rsertctu.u
aleRcl ttah lahse-halpeic nda -sbhattesee are eplmasex of reysdocan .ructteruss Tsih nac be thhuotg fo a tnamsinofeait of het laahp lx.eih
tNrAoeh ywa to gte ta it si aiv enna:tliomii
.A degnohry bgnnodi uldotwn aylrel acheng ensic etrhine eianaln nor igyecln ear oapB.r l ylG t&;g lAa sholtun'd eghnca who elropin si fidoedim (I aemn it ,LCDUO fi treeh asw a rtseic caridnnhe ro gehsom,int tub otn a etrga wsrn.e)aD nghoitn ot ainitcde atht lngeaocl odtrndeegai si aertled in speenros ot na AA uotsiitu.bnst Al,so in eht ocntxte fo IO cwih(h is the enespntgir a)pm,olticn we yealrad knwo ttah eht mrbloep n'dotse hvae igatnynh to od ithw d,ioteerngda mroe hiwt het caegnh ni oErucinr.tntust/cufe ntolsyHe dt'no nwok.
re’eHs eno wya ot e-soretascfiloenpim- deerd“scea bydongrdnho-e io:”arnftom m’I tno a gib afn of itsh eiln fo nri,ensgao tbu hatlnlceicy ainalne
as a sedi gpuor sha omre orednys*gh rfo tnaeploti engrydoh nndgibo nhta nlgciey
:
l:iaanen
C3H—
ne:icygl
—H
So, lchlae“nct”,iy ninalea
wdulo eritmp mero hn-reydonbdgo afmnroo,it hciwh tgihm waoll uyo ot eitenimla atht .icheco
Ttha a,dis ti esems tsamlo msespilibo ot uerl out tih(towu yerv ciahlecnt elgkedwon or oems dvpreoid peremilatnxe )aatd tath eth iglyhlst aglerr anianel
odes ton pmiiar hgonyder oibdgnn tbeenew agnoecll lumlesoce aiv strice as(ipta)l etire.cnnfere In prsleim ,esmrt ceins aaenlni
is ,eaglrr uoy ldowu hknit htta it mstu msoeowh rifnerete hwit eth nb-oydndogegihrn atth corusc htwi hte ydiwp-tel lngicey
.
---
lti*yctSr ne,iskpga ts’i not eht mebrnu fo gdhnyeors ubt aols teh etthsnrg of the loidep ttah alteitsafic eygorhnd obgni:dn a ynodrheg unodb to a gynrtols etlrcgenoieeatv ulecleom eilk lnroeufi lwil pe”p“ara oemr tispevoi ,dan htu,s bhreyongnddo- mroe orntsgyl with a rnaeby noxgye pacedom(r with a ngrhedyo cenndceto to bnoc,ra fro )lep.mxae
rFrthue aeg:indr
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).
https://www.ncbi.nlm.nih.gov/books/NBK26810/#_A3551_
I gmthi be itrnivheogkn it ,tub H nbdo nfatmoior of 'saa kmsae hte rynocasde uurettsrc of eht pontrei gacoll(ne in tshi sa.e)c ehT yGl to Ala sbtniuoutsti sdoe surtle in sesl H odnb tmi,orfaon btu of ldiuavdnii a'sa nto entebwe lcgonela eslmoclue ahtt( ihgmt eb oerm fro rreauanytq erustu)crt
raiyrmP crttsruue = oaimn cdia qsaeecrcdueSnyen o eursttcur = rtutuesrc omrefd hiwt a linsge naomi dcai ecnsuqee abt(e epdltae sthe,e lphaa ,xhile raeT)treycit sutrtcreu = tlelmuip rdyoescan trecssturu gtiriancten egethotr uiml(ptel tbae eedtalp heetss atkcsed on pot fo hace oreth, u)yQrtern tacear etutrrcsu = penirot urestrtuc eormfd frmo glodnfi fo lla aeyrtirt rtuusetscr to mkea gidbnin ise,st ce.t
neicS teh ailanen swa tup ni pacel of eth eGnc,yil eth irpamyr ttcreusru swa nlaueb to rfom na phlaa hlxie eisnc alpah xehil tcurteruss need a lcptriuraa nuqeseec (lgy - -x y) in oerrd ot ormf ndryghoe nbsdo to keep hte lhxei etbl.sa
wtah si ngaeclol ? a orecndasy ritenpo t.ruurcets
newh oyu eeomrv gnl,eyci eth most undatban oainm acid , mrof eth rurcsreop emeloclu ilwl oyu get a poprer yceodnars ctrtusreu ? NO
lyG si aporl, alAienn si nopaonrl adn oi.chyphdobr eensssMi nnostineraveovc ntamou.ti eTesh AsA hvae nedefirtf lhmeicac prtrsepioe wihch lead to isdpudert ptniore ldngiof resocnd(ay tes)cutur.r iSalmri to lGu - alV iisustntbuto in lSiekc Clle ieeDsas.
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$279$49I nkhit ti sha nmogehsit to od with ynicelg eud( ot its lmsal eszi ti anc fti in nyma psleca rehew teroh omnai sdcai cna ont dan cnhee it ovrdisep trcasruul“t sscapo”etmcn to hte angle,loc i..e utp a nikk in eth aphal .elihx) fI necgily is miepadlsc yb motshenig eles, I tdno’ inhkt npllgoo-reac acn omfr its rccerot nrsyoedca tu.eurrcst
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