Steven J. Evans
University of Newcastle
11 Papers
67 Citations
Steven J. Evans is an academic researcher from University of Newcastle. The author has contributed to research in topics: DNA & Endonuclease. The author has an hindex of 7, co-authored 11 publications.
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Papers
Mechanism and cleavage specificity of the H-N-H endonuclease colicin E9.
Ansgar J. Pommer,Santiago Cal,Anthony H. Keeble,Daniel Walker,Steven J. Evans,Ulrike C. Kühlmann,Alan Cooper,Bernard A. Connolly,Andrew M. Hemmings,Geoffrey R. Moore,Richard James,Colin Kleanthous +11 more
TL;DR: The data show that the H-N-H motif is an adaptable catalytic centre able to hydrolyse nucleic acid by different mechanisms depending on the substrate and metal ion regime.
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Nonlinear dynamics in ventricular fibrillation
TL;DR: A new statistical test is introduced that recovers significant dynamical patterns from smoothed lag plots that is used to show highly significant nonlinear dynamics in a stable canine model of ventricular fibrillation.
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Characterization of the quaternary structure and conformational properties of the human stem cell inhibitor protein LD78 in solution
Shilpa R. Patel,Steven J. Evans,Kevin Dunne,Graham C. Knight,Peter J. Morgan,Paul G. Varley,Stewart Craig +6 more
TL;DR: The results demonstrate that defined, homogeneous monomer and tetramer forms of LD78 can be prepared which display distinct conformational properties, and provide an insight into the pathway and molecular mechanics ofLD78 self-association.
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Effects of non-conservative changes to tyrosine 76, a key DNA binding residue of DNase I, on phosphodiester bond cleavage and DNA hydrolysis selectivity.
TL;DR: The DNA cleavage selectivity of the Y76E, Y 76L, Y76Q and Y76W mutants were little altered as compared with the wild-type enzyme as measured using the cutting patterns of a 160 base-pair Escherichia coli Tyr T promoter DNA fragment, confirming earlier observations that showed that this tyrosine has little role inDNA cleavage specificity.
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Site-directed mutagenesis of phosphate-contacting amino acids of bovine pancreatic deoxyribonuclease I.
TL;DR: A comparison of DNase I variants from several species suggests that certain amino acids, which allow interaction with phosphates (positively charged or hydrogen bonding), are tolerated and suggests that phosphate binding residues play no role in the selection of DNA substrates.
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