Richard Greaves

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The database of protein structures contains representatives from organisms with a range of growth temperatures. Various properties have been studied in a search for the molecular basis of protein adaptation to higher growth temperature. Charged groups have emerged as key distinguishing factors for proteins from thermophiles and mesophiles. A dataset of 291(More)
Electrostatics calculations with proteins that are uniformly charged over volume can aid enzyme/non-enzyme discrimination. For known enzymes, such methods locate active sites to within 5% on the enzyme surface, in 77% of a test set. We now report that removing the dielectric boundary improves active site location to 80%, with optimal discrimination between(More)
The rate of protein structures being deposited in the Protein Data Bank surpasses the capacity to experimentally characterise them and therefore computational methods to analyse these structures have become increasingly important. Identifying the region of the protein most likely to be involved in function is useful in order to gain information about its(More)
Charges are important for hyperthermophile protein structure and function. However, the number of charges and their predicted contributions to folded state stability are not correlated, implying that more charge does not imply greater stability. The charge properties that distinguish hyperthermophile proteins also differentiate psychrophile proteins from(More)
JOHN FORRESTER, RICHARD GREAVES, HOWARD NOBLE, AND RICHARD TAYLOR York Centre for Complex Systems Analysis, Ron Cooke Hub, University of York, York, YO10 5GE, United Kingdom; Department of Computer Science, University of York, York, YO10 5GE, United Kingdom; Oxford University IT Services, 13 Banbury Road, Oxford, OX2 6NN, United Kingdom; and Stockholm(More)
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