Zobrazeno 1 - 10
of 184
pro vyhledávání: '"Roy M. Daniel"'
Autor:
Roy M. Daniel, Rosalind A. Reeves, P.R. Choudhary, Elizabeth M. Hardiman, Moreland D. Gibbs, Peter L. Bergquist
Publikováno v:
New Biotechnology. 27:795-802
Xylanases have several industrial uses, particularly in baking, modification of animal feed and in pulp bleaching in the paper industry. Process conditions in kraft pulp bleaching generally favour an enzyme that is active at high pH values. The activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1983548980dcbbc2c66baa546d400932
https://doi.org/10.1016/j.nbt.2010.06.004
https://doi.org/10.1016/j.nbt.2010.06.004
Autor:
Roy M. Daniel, Michael J. Danson
Publikováno v:
Trends in Biochemical Sciences. 35:584-591
The two established thermal properties of enzymes are their activation energy and their thermal stability, but experimental data do not match the expectations of these two properties. The recently proposed Equilibrium Model (EM) provides a quantitati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c8a4f101ad209da8ad8c1eaea3e846b
https://doi.org/10.1016/j.tibs.2010.05.001
https://doi.org/10.1016/j.tibs.2010.05.001
Publikováno v:
International Journal of Environmental Analytical Chemistry. 88:1063-1075
While direct toxicity assessment (DTA) is now widely recognised as a useful tool for environmental risk assessment, many existing tests fail to meet end-user needs. This article describes the significant progress made to the MICREDOX® DTA assay, dev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2681ce74092798da37d1f2519716fb65
https://doi.org/10.1080/03067310802248028
https://doi.org/10.1080/03067310802248028
Autor:
Barbara J. Campbell, Mihailo Kaplarevic, Roy M. Daniel, Stephen Craig Cary, Robert A. Feldman, Joseph J. Grzymski, Charles Kai-Wu Lee, Guang R. Gao, Alison E. Murray, Amir Ghadiri
Publikováno v:
Proceedings of the National Academy of Sciences. 105:17516-17521
Hydrothermal vent ecosystems support diverse life forms, many of which rely on symbiotic associations to perform functions integral to survival in these extreme physicochemical environments. Epsilonproteobacteria , found free-living and in intimate a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78c52628462eca8fbe96b67a71d24660
https://doi.org/10.1073/pnas.0802782105
https://doi.org/10.1073/pnas.0802782105
Publikováno v:
Biophysical Journal. 94:4812-4818
The temperature dependence of the dynamics of mesophilic and thermophilic dihydrofolate reductase is examined using elastic incoherent neutron scattering. It is demonstrated that the distribution of atomic displacement amplitudes can be derived from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aacc23c213b74cf415edce6a0b2fd5e
https://doi.org/10.1529/biophysj.107.121418
https://doi.org/10.1529/biophysj.107.121418
Publikováno v:
Biochemical Society Transactions. 35:1543-1546
Arising from careful measurements of the thermal behaviour of enzymes, a new model, the Equilibrium Model, has been developed to explain more fully the effects of temperature on enzymes. The model describes the effect of temperature on enzyme activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6a20b73507a990c6e5574ac6f067faa
https://doi.org/10.1042/bst0351543
https://doi.org/10.1042/bst0351543
Publikováno v:
Extremophiles. 12:51-59
The two established thermal properties of enzymes are their activation energy and their thermal stability. Arising from careful measurements of the thermal behaviour of enzymes, a new model, the Equilibrium Model, has been developed to explain more f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43914024e57cdbc15f795e8d512ea329
https://doi.org/10.1007/s00792-007-0089-7
https://doi.org/10.1007/s00792-007-0089-7
Autor:
Robert Eisenthal, S. Craig Cary, David J. Saul, Michael J. Danson, Charis Shepherd, Roy M. Daniel, Michelle E. Peterson, Charles Kai-Wu Lee
Publikováno v:
The FASEB Journal. 21:1934-1941
The "Equilibrium Model" has provided new tools for describing and investigating enzyme thermal adaptation. It has been shown that the effect of temperature on enzyme activity is not only governed by deltaG(double dagger)(cat) and deltaG(double dagger
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd0afd6500358d8bf9521a7b8e0c7e2d
https://doi.org/10.1096/fj.06-7265com
https://doi.org/10.1096/fj.06-7265com
Autor:
Roy M. Daniel, Rachel V. Dunn, Jeremy C. Smith, Moeava Tehei, Vandana Kurkal-Siebert, John L. Finney
Publikováno v:
Journal of Non-Crystalline Solids. 352:4387-4393
Recent measurements have demonstrated enzyme activity at hydrations as low as 3%. The question of whether the hydration-induced enzyme flexibility is important for activity is addressed by performing picosecond dynamic neutron scattering experiments
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::71cad482fdfde89c2b06eaa302d485bb
https://doi.org/10.1016/j.jnoncrysol.2006.01.115
https://doi.org/10.1016/j.jnoncrysol.2006.01.115
Publikováno v:
Trends in Biotechnology. 24:289-292
The way that enzymes respond to temperature is fundamental to many areas of biotechnology. This has long been explained in terms of enzyme stability and catalytic activation energy, but recent observations of enzyme behaviour suggest that this pictur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e477573d1972db0fd84966be8830b7da
https://doi.org/10.1016/j.tibtech.2006.05.004
https://doi.org/10.1016/j.tibtech.2006.05.004