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, B. W. (1975). "Comparison of the predicted and observed secondary structure of T4 phage lysozyme". Biochimica et Biophysica Acta (BBA) - Protein Structure. 405 (2): 442–451. doi:10.1016/0005-2795(75)90109-9. PMID1180967.
^Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H (1972). "Structure of thermolysin". Nature New Biology. 238 (80): 41–43. doi:10.1038/newbio238041a0. PMID18663850.
^Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW (1981). "Structure of the cro repressor from bacteriophage λ and its interaction with DNA". Nature. 290 (5809): 754–758. doi:10.1038/290754a0. PMID6452580. S2CID4360799.
^Fenna RE, Matthews BW (1975). "Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola". Nature. 258 (5536): 573–577. doi:10.1038/258573a0. S2CID35591234.