Random Library Of Myoglobin Mutants Probes Protein Properties

Abstract

Chemists at Stanford University have created a random library of single amino acid mutants of myoglobin to discover new ligand binding pathways in the protein. In addition to providing new insights into the function of myoglobin—the oxygen storage and transport protein in muscle—the approach is likely to be useful in probing structure-function relationships in other proteins. Conceptually, this is a simple idea which had almost no chance of working, but it did, says Steven G. Boxer, the chemistry professor at Stanford who directed the research. The approach developed by Boxer and Xiaohua Huang, a graduate student, differs sharply from site-directed mutagenesis, the technique that has revolutionized the study of structure-function relationships in proteins over the past decade. In site-directed mutagenesis, the researcher selects a particular amino acid residue in a protein and systematically inserts different amino acids at that position. Characterizing the properties of the mutant proteins sheds light ...