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Article

Effects of metal binding affinity on the chemical and thermal stability of site-directed mutants of rat oncomodulin.

Biophysical chemistry - 20 Apr 1998

Zheng L, Hogue C W, Brennan J D

Abstract excerpt

Tryptophan fluorescence was used to study the stability and unfolding behavior of several single tryptophan mutants of the metal-binding protein rat oncomodulin (OM); F102W, Y57W, Y65W and the engineered protein CDOM33 which had the 12 residues of the CD loop replaced with a more potent metal binding site. Both the thermal and the chemical stability were improved upon binding of metal ions with the order apo <...

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Identifiers

PMID: 9648206
DOI: 10.1016/s0301-4622(98)00096-9

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