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Tyrosine helix-coil transition

Tphe complexing of virtually all purines with aromatic molecules seems - to have far-reaching biological significance. For example, it is known that caffeine affects the rates of many enzymatic reactions (e.g., 0.01, 0.05, and 0.10M caffeine will inhibit salivary amylase 29, 54, and 72% respectively) (12), and purine can decrease the helix-coil transition temperature of the proteins bovine serum albumin and lysozyme (2). It is not unreasonable to expect the involvement of caffeine-aromatic and purine-aromatic complexes because caffeine derivatives and purine complex with the aromatic amino acids tyrosine, phenylalanine, and tryptophan (2). (In fact tryptophan forms a stable 1 to 1 crystalline complex in 0.5M theophylline glycol.)... [Pg.242]

Polyaminoacids studied are poly-T-histidine (pH-induced, j5->coil transition in aqueous solution) [5] and poly-L-tyrosine (a-helix -> coil transition in mixed organic solvents) [8]. [Pg.116]


See other pages where Tyrosine helix-coil transition is mentioned: [Pg.437]    [Pg.457]    [Pg.438]    [Pg.267]    [Pg.231]    [Pg.63]    [Pg.524]    [Pg.373]   
See also in sourсe #XX -- [ Pg.474 ]




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Helix-coil transition

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