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Peptide backbone solute effects

Lysine also may form complexes with anionic ligands and thereby increase Am values. In addition, lysine may have an unfavorable effect on protein structure. Because it has a considerable hydrophobic moment, it may interact with hydrophobic sites on the protein, leading to perturbation of structure. Compatible solutes lack a propensity for interacting with peptide backbone linkages or amino acid side-chains, as discussed later. [Pg.237]

The next question to be addressed carries the mechanistic analysis one step further by asking what components of proteins—the side-chains or the peptide backbone linkages—are responsible for solute effects on structure. The answer to this question, which comes from studies... [Pg.246]

See other pages where Peptide backbone solute effects is mentioned: [Pg.74]    [Pg.290]    [Pg.303]    [Pg.142]    [Pg.214]    [Pg.222]    [Pg.245]    [Pg.247]    [Pg.248]    [Pg.45]    [Pg.264]    [Pg.282]    [Pg.143]    [Pg.23]    [Pg.151]    [Pg.26]    [Pg.423]    [Pg.575]    [Pg.119]    [Pg.42]    [Pg.213]    [Pg.434]    [Pg.81]    [Pg.535]    [Pg.311]    [Pg.429]    [Pg.118]    [Pg.262]    [Pg.242]    [Pg.98]    [Pg.199]    [Pg.465]    [Pg.277]    [Pg.139]    [Pg.61]    [Pg.507]    [Pg.159]    [Pg.175]    [Pg.178]    [Pg.298]    [Pg.23]    [Pg.476]    [Pg.112]    [Pg.62]    [Pg.903]    [Pg.177]    [Pg.373]    [Pg.177]    [Pg.471]   
See also in sourсe #XX -- [ Pg.246 , Pg.247 , Pg.248 ]



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