Oxidation of tryptophans in an interhelical hydrophobic cluster of myoglobin alters the thermodynamics of the denaturation transition.


Model folding studies of sperm whale myoglobin have illustrated the presence of hydrophobic interfacial regions between elements of secondary structure. The specific oxidation of two tryptophan residues, in the A-H helix contact of sperm whale myoglobin, to the less hydrophobic oxindolylalanine residues is utilized to probe the contribution of hydrophobic… (More)


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