Robert Joseph Paton Williams, D.Phil., FRS

University of Oxford University of Oxford, Oxford, United Kingdom 
nuclear magnetic resonance spectroscopy, enzymology
"Robert Joseph Paton Williams"

(1926 - 2015)
DOI: 10.1007/s00775-015-1328-5
DOI: 10.1042/BIO03704038
DOI: 10.1098/rsbm.2016.0020

Mean distance: 8.19


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H. Allen O. Hill grad student Oxford
Stephen Mann grad student Oxford
Geoffrey  R. Moore grad student Oxford
Andrew Thomson grad student
Michael T. Pope grad student 1954-1957 Oxford
C. Keith Prout grad student 1957-1959 Oxford
Brian R. James grad student 1960 Oxford
Andrew James Thomson grad student 1965 Oxford
Peter Day grad student 1961-1965 Oxford
Tony Orchard grad student 1967 Oxford
Peter J. Sadler grad student 1972 Oxford
Antonio V. Xavier grad student 1972 Oxford
Christopher M. Dobson grad student 1976 Oxford
Nigel J. Clayden grad student 1981 Oxford
Rachel E. Klevit grad student 1981 Oxford
Carole C Perry grad student 1981-1985 Inorganic chemistry Laboratory, Oxford University
Peter E. Wright post-doc 1972-1976 Oxford
Gary J. Pielak post-doc 1986-1989 Oxford
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Cockle S, Davies S, Foster M, et al. (2010) Cobalt as a functional group in enzymes. The Biochemical Journal. 117: 54P
Coyle CM, Vogel KM, Rush TS, et al. (2003) FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy. Biochemistry. 42: 4896-903
Gray HB, Malmström BG, Williams RJ. (2000) Copper coordination in blue proteins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 551-9
Armstrong FA, Williams RJ. (1999) Thermodynamic influences on the fidelity of iron-sulphur cluster formation in proteins. Febs Letters. 451: 91-4
Williams RJ. (1996) Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. European Journal of Biochemistry. 234: 363-81
Veitch NC, Williams RJ, Bone NM, et al. (1995) Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme C mutants with alanine replacing either Phe142 or Phe143. European Journal of Biochemistry / Febs. 233: 650-8
João HC, Williams RJ. (1993) The anatomy of a kinase and the control of phosphate transfer. European Journal of Biochemistry. 216: 1-18
Gao Y, Veitch NC, Williams RJ. (1992) The value of chemical shift parameters in the description of protein solution structures. Journal of Biomolecular Nmr. 1: 457-71
Veitch NC, Williams RJ, Bray RC, et al. (1992) Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys. European Journal of Biochemistry / Febs. 207: 521-31
João HC, Taddei N, Williams RJ. (1992) Investigating interdomain region mutants Phe194----Leu and Phe194----Trp of yeast phosphoglycerate kinase by 1H-NMR spectroscopy. European Journal of Biochemistry. 205: 93-104
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