I ,euidrgf -i-XeygYlnc si itnlhclycae cdsnederio a “rpirmay oanim cdia uetrrcuts of a epr”iont icens eht eioidtinnf of a rPiyarm srrcuuett fo a nrotpei is “a lnraie iacnh fo namio das”i.c fI uoy smse whit teh Prryiam teustucrr, sa ni eth ntouisqe t,mes oyu cnotan ofmr hte enycaoSdr cesutrtru fo het oitpre,n wichh is netdiedrem by the dgbgyiroh-nndnoe cihwh rosccu enebetw teh pediept cbakbeno, ddepiennetn fo teh R opsr.ug I heop isth adme nsese.
roFm dkiepiawi: Sreyn“oadc rurstcetu is floamylr idnfdee by eth eaptnrt fo hegoynrd sndob webetne het noima dhygnroe adn olacrxyb xgneoy maots in eht epeidtp kbcbeano.” (mhepssia nmi)e
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 ugsy and i euqot frmo eesp/lgotrosluhis4/i2obcr-epaeetmcs.sepocwd/iat.hwisrf1teow0tt/mtn:/
%09" vahe na dltiiaeienbf geitcne mtutoina
CLO 1A1 adn OCL 21A
cuaes
s romaalnb gnaclleo iigsnkn-oslcr via a eyiclng oisustubntit ni eht rlaonoglcpe mcuelelo "
hichw anmes that IO hsa a gniecly soittsuntiub adn oehtferr its ebunal to frmo a cyrsnedoa tucrsu.uter
eDu ot clsnygei' llsam ,eizs it ertsaec "knks"i in teh inoma iacd cequnees. hTese knsik era ndedee ot etrocyclr frmo eht seyarcdno crurse.utt
terOh nss:rwae
Yly--GX is ckbbeaon orf golancel lpaah c.naih 3 loglenac ahlpa acisnh prlasi to form ilerpt h.ilxe neciyGl ash on R r,gpou lwonialg orf ifibelxilyt dna mafotiorn of reptil xi.ehl No ngleyci espvrent hsit nioustuonc irpnsi,gla neitgneprv the frnaoitmo of lalnoceg sydocrane rrtc.useut
claeRl hatt haasp-eillhce dna sbeestheta- ear mlepeaxs fo csdanreyo tse.trucsur Tshi nac be othtuhg of a nifmoatistane of eht lhaap hli.xe
reohNAt ywa ot get ta it si via inno:teilami
.A hrygnode dgbnion ondwtul lalyre gcnaeh seicn nethrie enailan onr linecyg aer roap.Bl Gly t;&g laA us'lnhdto nhaceg who pnoreil si dfiemiod I( eamn ti ODULC, if rehet was a ecsrti niardenhc or nmesitho,g but tno a eagtr wre)nsaD. hotnngi to aicntedi tath gceanllo ngeitoaeddr is raedlte ni enpsorse ot an AA ttoinsbusut.i oAl,s ni teh tnoxetc of OI hi(cwh is eht eesginptnr ),milnaocpt ew adearyl owkn atht eth leprbom et'dsno ahev tyghainn to od wtih eirnetgd,doa moer hwit eht heangc ni sttiEnc /ruouerfuc.nt eysoHnlt o'ntd nok.w
eH’rse eno way to snafmisclteo--eeripo rdeacees“d dy-ogrndohneb of:rtom”nai mI’ not a ibg fna of tish lnei of nia,ergosn tub ncicaeylhtl laaienn as a seid gopru ahs emor orehgynsd* for itpotalne rgenoyhd ngibdno ahnt gelciyn:
neia:aln CH3—
iey:nlcg —H
oS, etlcih“alync”, anlnaei oudwl mtierp mero yonbe-ordnhdg ar,oioftnm which ihmtg olwal oyu to nliiaeetm ahtt ho.iecc
htTa sia,d it sesem motsla mlipssiboe ot urle tou tuioh(tw ryev nlcahitec elgokwdne ro mose iodrepvd eaenxerlitpm daat) hatt het slitglyh elrgar nainale dsoe ont mirapi nreoghyd ngibdno tewnebe ocelngla lomceseul via ertisc s)(apliat erenet.cnrife nI ermilsp ,tsmer sceni ilenana si ler,agr you oudlw iknth taht it sumt moeoshw trnfreeie itwh eht d-bonrgignoeyhnd atht ocusrc ihtw eht wdelp-tyi lynecig.
---
tilt*rSyc sep,ikang i’ts ton eht bemurn fo rseygondh but aslo het htgtrnse fo the epidlo ttha cfietasiatl ngeryhod og:dinbn a ngoyherd ounbd to a nrltygso nltvegeoetcirea elulcome klie ulfoenir lliw ”“paerap omer epoivsit ,dna tuhs, ddyngeo-hnrbo ermo lysotnrg iwth a yrebna oyngxe ceapo(rmd htiw a hogernyd ecntnoedc to r,bacno rof .ale)pmex
rFtuerh aigenr:d
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 migth be tnrevignihok it tu,b H nbod moarniotf fo asa' makse eht dcaesnyor suectutrr of eth ntireop elalc(ong ni ihst ase.c) Teh Gyl to aAl utiisuntstbo sdoe srtlue in lsse H nbdo niartoom,f ubt of ldaidunvii 'asa tno beteenw aelnolcg seluelmco h(tta hitgm eb orem ofr yuqnraerta )cruutrtes
yarmirP rsuctteru = manoi cadi yqnsoeeeudnS racce stetcurru = rcetustur ofedmr tihw a ensigl naoim daic eueqnecs (teab pleedat tesh,e phlaa ilxh,e Tte ceay)itrr sutrtucre = lpulmite crydsaeno rscstueurt tgietrcnian heetogrt mtul(plie bate lpetdea tseesh dcatkse on pot fo ceha rh,ote te)rareucy tnQar trsuurcet = pnireot struucret edmorf orfm ndilofg fo lal reyiratt uttrssecur ot kaem gnndiib e,isst te.c
icnSe eth ennilaa wsa utp in pleca of eht iGneycl, eth mrpiyra cretsuutr asw nbuela to omrf an plaha ixhle isecn aphla ihxle rutecursts ndee a arliuaptcr ecsueeqn (ylg - x- )y in rerdo ot rmof hneogyrd dnsob to kepe the hliex lasbt.e
htaw is aegnlclo ? a conyaerds teiporn sr.trucetu
ewhn uoy orvmee ,ligneyc the osmt nubtaadn nomai iadc , romf the crsrropue oleuecml iwll you gte a rprepo arosecynd utturcres ? NO
Gly si oa,rpl inAelan si ronlnapo nda dhp.icryboho esenssiM oirvnsoenevactn ouman.itt shTee AsA hvea irdnfteef almihcec eeptosrpri hwchi eadl to spiurddte treonpi ngdifol cno(ysrdae us.)rutertc lmSairi ot uGl - alV ssiotubttniu in ciekSl eCll D.asiese
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$279$49I tikhn it sha hnteismog ot od whti niegcly e(du ot tis llasm eszi ti nac tif ni amyn lpeacs rheew thero iaomn sdaci acn otn dan enceh it vrdoespi lu“rastruct cssetcnpom”a to eth egalcln,o e.i. tpu a kkin in eht halpa .xleh)i fI lyecgni is slpedacmi by ohgntemsi ,sele I n’odt tinkh copoega-lrln acn fmro ist rtercoc dcaerynso c.ruusrtet
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