Brian Matthews (biochemist)

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Brian W. Matthews
Born
1938 (age 79–80)[1]
Mount Barker, South Australia
Alma mater
University of Adelaide
Known for


  • Matthews correlation coefficient[2]


Scientific career
Institutions

  • University of Cambridge

  • University of Oregon

  • Howard Hughes Medical Institute


Academic advisors
David M. Blow[3]

Website
molbio.uoregon.edu/matthews/


T4 lysozyme ribbon schematic (from PDB 1LZM)


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.


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 1975.[2] 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 is the editor of the scientific journal Protein Science.



References




  1. ^ Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. (2009). "Structural Studies of Thermolysin: the Work of Brian W. Matthews". The Journal of Biological Chemistry. 284 (26): e8–e9. 


  2. ^ ab 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. 


  3. ^ "Blow on AcademicTree.org". 


  4. ^ ,Matthews BW (1966). "The determination of the position of anomalously scattering heavy atom groups in protein crystals". Acta Crystallographica. 20: 230–239. doi:10.1107/S0365110X6600046X. 


  5. ^ Matthews BW, Remington SJ (1974). "The three dimensional structure of the lysozyme from bacteriophage T4". Proc. Natl. Acad. Sci. USA. 71: 4178–4182. doi:10.1073/pnas.71.10.4178. PMC 434353 Freely accessible. 


  6. ^ Baase WA, Liu L, Tronrud DE, Matthews BW (2010). "Lessons from the lysozyme of phage T4". Protein Science. 19 (4): 631–41. doi:10.1002/pro.344. PMC 2867005 Freely accessible. PMID 20095051. 


  7. ^ 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. 


  8. ^ 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. PMID 6452580. 


  9. ^ Fenna RE, Matthews BW (1975). "Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola". Nature. 258: 573–577. doi:10.1038/258573a0. 



External links


  • Brian Matthews at The Institute of Molecular Biology at the University of Oregon

  • HHMI Alumni Scientists

  • Molecule of the Month: Lysozyme

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