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Nat Struct Biol. 1994 Apr;1(4):226-9.

Discovery of new ligand binding pathways in myoglobin by random mutagenesis.

Author information

1
Department of Chemistry, Stanford University, California 94305-5080, USA.

Abstract

A random library of single amino acid mutants of myoglobin was generated using a highly efficient, single-base-misincorporation random mutagenesis method to discover new ligand-binding pathways in myoglobin. A surprisingly large fraction of the library exhibits ligand-binding kinetics that are substantially different from the wild-type protein. In addition to residues 45, 64 and 68, which comprise the best studied ligand-binding pathway single mutations of several other clusters of residues far away from that pathway are discovered which profoundly affect the ligand-binding kinetics. These results provide a new approach to explore the relationship between the fluctuations in protein structure and function.

PMID:
7656050
DOI:
10.1038/nsb0494-226
[Indexed for MEDLINE]

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