Dr. Brian Matthews is a preeminent molecular biophysicist whose pioneering work has fundamentally shaped the field of structural biology and protein science. Currently serving as Courtesy Professor of Physics at the University of Oregon, he has been a cornerstone of the Institute of Molecular Biology since joining the institution in 1969. Educated at the University of Adelaide where he earned his PhD in 1964, Matthews later made significant contributions to x-ray crystallographic methodology during his time at the University of Cambridge before establishing his influential research program at Oregon. His distinguished career has been recognized with his election to the National Academy of Sciences in 1986 and his appointment as a Howard Hughes Medical Institute Investigator from 1989 to 2008, cementing his reputation as a leading figure in biophysical research.
Dr. Matthews revolutionized our understanding of protein stability through his systematic creation and analysis of hundreds of T4 lysozyme mutants, establishing it as the most commonly represented protein structure in the Protein Data Bank. His meticulous work deciphered the fundamental energetic and structural effects of mutations in proteins, transforming how scientists understand protein folding and thermal stability. Beyond his landmark lysozyme studies, he solved early structures of thermolysin from thermophilic bacteria, the lambda Cro repressor DNA-binding protein, and the bacteriochlorophyll protein, advancing multiple frontiers in structural biology. His contributions extend beyond biochemistry, as he introduced the Matthews correlation coefficient in 1968, which has become a standard measure for evaluating binary classification quality in machine learning and data science applications.
As editor of the journal Protein Science, Dr. Matthews has shaped the dissemination of knowledge in structural biology for decades while maintaining a rigorous research program that addresses fundamental questions about protein folding, stability determinants, and molecular interactions. His laboratory continues to employ x-ray crystallography in concert with complementary techniques to unravel how proteins spontaneously fold into biologically active configurations and how they interact with DNA and other molecules. The precision and methodological rigor of his experimental approach have established gold standards for structural studies of protein engineering and stability. Dr. Matthews' enduring influence is evident in the widespread adoption of his methodologies and the generations of scientists he has trained, ensuring that his contributions to understanding the physical principles governing biological macromolecules will continue to advance the field for years to come.
