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Peptide ligands hydrophobic effect

Changes in the magnitude of In k with solvent concentration in peptide-ligand interactions in RPC involving hydrophobic effects can also be related in solvophobic terms to the chemical potential, Ap°, for the process, or to the surface tension, y, of the mobile phase through the following expressions ... [Pg.564]

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]

See other pages where Peptide ligands hydrophobic effect is mentioned: [Pg.139]    [Pg.139]    [Pg.155]    [Pg.550]    [Pg.551]    [Pg.556]    [Pg.558]    [Pg.559]    [Pg.584]    [Pg.607]    [Pg.445]    [Pg.377]    [Pg.117]    [Pg.152]    [Pg.39]    [Pg.60]    [Pg.63]    [Pg.292]    [Pg.403]    [Pg.234]    [Pg.403]    [Pg.37]    [Pg.185]    [Pg.370]    [Pg.536]    [Pg.24]    [Pg.38]    [Pg.80]    [Pg.439]    [Pg.552]    [Pg.553]    [Pg.564]    [Pg.567]    [Pg.568]    [Pg.573]    [Pg.577]    [Pg.578]    [Pg.580]    [Pg.596]    [Pg.618]    [Pg.155]    [Pg.84]    [Pg.536]    [Pg.770]    [Pg.58]    [Pg.175]    [Pg.255]   
See also in sourсe #XX -- [ Pg.60 , Pg.61 ]



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Hydrophobic Effect of Peptide and Related Ligands

Hydrophobic effect

Ligand effect

Ligand effective

Ligands, hydrophobicity

Peptides hydrophobicity

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