I fugdier, cXl-Yegyn-i si lcintlaehyc dsedrcneoi a m“ripayr inoma iacd ucsturret of a retoinp” icnse het iotnedfnii fo a iarryPm uerttrucs of a tnopier si a“ iralen nciha fo mnaoi ”sacd.i If yuo ssem wiht eth yrmiaPr turtcsre,u as ni eth iouqenst ,mste uoy nacton ormf eht Scoyderan rustucrte of eht ,etrinpo hcwhi si rddniteeme yb the hnegonbidnoy-gdr iwhhc ursocc eenewtb het etpiped eaonbkcb, epedntnndie fo het R s.gopur I peoh thsi aemd sne.es
Form dikweipia: onSrcdeya“ rutuetrsc si moylrfla fdedine yb hte pterant of egnyohdr donsb weetben eth imnoa ydognreh nda lbxorcay ngxeoy omsat in teh edtppie knbeobac.” isapem(sh i)nme
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.
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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).
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icSne het aennila asw put in epacl of the cln,yiGe teh rryaipm tscutrure swa nueabl ot mofr an hpaal xeihl niecs pahal hexil rrttsseuuc deen a tirlaacrpu ucseeqne gyl( - -x )y in rrdeo ot fmor yhgoerdn nosdb to epek eht elhxi ebl.sat
tawh si lacgnloe ? a eadocsnry nrptoei urst.ucter
nehw yuo overme ,lnecgiy eth sotm dntbaanu inamo iadc , rmfo het eporrscru eemoulcl llwi ouy teg a prpeor oeadrsnyc ucrtrseut ? NO
lGy si orlpa, aenilAn si rplonnao nad rhpc.byiohdo nisseesM voncvnsetrnioae otamtn.iu eehTs sAA ehva tnfiedrfe clmiehca stpreiproe hichw edal to dtusieprd rpeiton oldnfgi y(econsadr uec)turt.sr iSalimr ot lGu - laV otsibtiuusnt in eiSkcl lelC sisa.eeD
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