Brian Matthews (biochemist)
Australian biochemist and biophysicist / From Wikipedia, the free encyclopedia
Brian W. Matthews is a biochemist and biophysicist educated at the University of Adelaide, contributor to x-ray crystallographic methodology[4] at the University of Cambridge, and since 1970 at the University of Oregon as Professor of Physics and HHMI investigator in the Institute of Molecular Biology.
Brian W. Matthews | |
---|---|
Born | 1938 (age 85ā86)[1] |
Alma mater | University of Adelaide |
Known for | |
Scientific career | |
Institutions | |
Academic advisors | David M. Blow[3] |
Website | molbio |
He created hundreds of mutants of T4 lysozyme (making it the commonest structure in the PDB), determined their structure by x-ray crystallography and measured their melting temperatures. Starting from questions about the basis of "temperature-sensitive" mutations,[5] his work has explicated much about the general energetic and structural effects of mutations in proteins.[6] He also solved early structures of the thermophilic bacterial enzyme thermolysin,[7] the helix-turn-helix DNA-binding transcription factor lambda Cro repressor,[8] and the light-antenna bacteriochlorophyll protein.[9]
Beyond his contributions to biochemistry, Matthews is also known in the machine learning community for the Matthews correlation coefficient, which he introduced in a paper in 1968.[10] The coefficient is used as a measure of the quality of binary (two-class) classifications.
Matthews has been a member of the National Academy of Sciences since 1986. He was the editor of the scientific journal Protein Science.