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Hydrophobic interactions between protein nonpolar groups

Protein tertiary structure results from hydrophobic interactions between nonpolar side groups and hydrogen bonds between polar side groups that stabilize folding of the secondary structure into a compact overall arrangement, or conformation. [Pg.68]

The hydrophobic interaction between nonpolar R groups is one of the forces that helps maintain the proper three-dimensional shape of a protein. [Pg.559]

Hydrophobic interactions are interactions between two nonpolar amino acids that have nonpolar R gronps. Within a protein, the amino acids with nonpolar R groups are pnshed away from the aqneons environment to form a hydrophobic center at the interior of the protein molecnle. [Pg.565]


See other pages where Hydrophobic interactions between protein nonpolar groups is mentioned: [Pg.375]    [Pg.231]    [Pg.3]    [Pg.375]    [Pg.669]    [Pg.178]    [Pg.371]    [Pg.177]    [Pg.193]    [Pg.193]    [Pg.273]    [Pg.57]    [Pg.338]    [Pg.193]    [Pg.371]    [Pg.197]    [Pg.42]    [Pg.7]    [Pg.522]    [Pg.269]    [Pg.1668]    [Pg.1092]    [Pg.669]    [Pg.671]    [Pg.80]    [Pg.1017]    [Pg.372]    [Pg.10]    [Pg.311]    [Pg.35]    [Pg.354]    [Pg.63]    [Pg.54]    [Pg.11]    [Pg.50]    [Pg.332]    [Pg.133]    [Pg.599]    [Pg.33]    [Pg.126]    [Pg.31]    [Pg.85]    [Pg.56]    [Pg.65]    [Pg.95]    [Pg.153]   
See also in sourсe #XX -- [ Pg.230 ]




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Hydrophobic groups

Hydrophobic interactions

Hydrophobic protein interactions

Hydrophobic proteins

Hydrophobic/hydrophobicity interactions

Hydrophobized interaction

Interaction group

Nonpolar

Nonpolar groups

Nonpolar interactions

Nonpolarized

Proteins groups

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