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mFor pdaiwkiie: eoycndarS“ utucrstre is lrmayofl efedind by eht eptartn of henrodyg obnds netweeb the imnoa hregnoyd dan xyracbol yxneog smato ni het dtepeip bnboakce”. p(saeimsh )meni
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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orehAtN ywa to gte at it si iav nti:aiomnlei
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---
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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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awht si olngacle ? a nyaorcesd oinpter ur.rtcuets
ehwn ouy vermeo ecliy,ng eht otms tdunbnaa amoin idca , fmro teh roreurcsp ceomeull illw oyu tge a rroppe asnyroedc tetsucrru ? ON
Gly is lpora, nAaniel is aolnnopr dan cyobpid.ohhr Mieessns ncvoornesnitvea muot.itan seehT sAA heav fdifetrne aielcchm eeporstpri ihhcw elad ot upidestrd oentirp fdlgino ya(cesndro tsr.e)urcut maiSrli to ulG - Val usbisnitotut ni cSklie Clel aiDeses.
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$279$49I tkinh ti has inhgestom ot od htiw yilcnge e(du to sti sllam zeis it can itf ni nmay lspcea weerh oerht omnai sadci acn ton adn nceeh ti sdpoevri tualr“csurt escnptm”caos to the cel,ganlo ie.. tpu a kkni ni the lphaa l)ixe.h If ngiecly is aelpdimsc by gnoemihst s,lee I no’td ntikh cnogelrpo-la can fmor tsi trrceco noydresca erusrtu.tc
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