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Paul C Engel

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Biochimica Et Biophysica Acta|May 26, 2009
Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stabilityXiao-Tao Wang, Paul C Engel
BMC Biotechnology|March 17, 2009
An optimised system for refolding of human glucose 6-phosphate dehydrogenaseXiao-Tao Wang, Paul C Engel
FEMS Microbiology Letters|February 26, 2008
Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coliMichael A Sharkey, Paul C Engel
FEBS Letters|May 13, 2008
Homotropic allosteric control in clostridial glutamate dehydrogenase: different mechanisms for glutamate and NAD+?Muaawia A Hamza, Paul C Engel
Proteins|May 9, 2009
Modular coenzyme specificity: a domain-swopped chimera of glutamate dehydrogenaseMichael A Sharkey, Paul C Engel
The FEBS Journal|November 12, 2013
The specificity and kinetic mechanism of branched-chain amino acid aminotransferase from Escherichia coli studied with a new improved coupled assay procedure and the enzyme's potential for biocatalysisXuejing Yu, Xingguo Wang, Paul C Engel
FEMS Microbiology Letters|February 25, 2005
Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli hostJohn B Carrigan, Suzie Coughlan, Paul C Engel
The FEBS Journal|May 14, 2011
Re-engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzymeMarina Capone, David Scanlon, Joanna Griffin, et al.
The FEBS Journal|July 25, 2007
The contribution of tryptophan residues to conformational changes in clostridial glutamate dehydrogenase--W64 and W449 as mediators of the cooperative response to glutamateMuaawia A Hamza, Stephen R Martin, Paul C Engel
The FEBS Journal|September 1, 2005
Two novel variants of human medium chain acyl-CoA dehydrogenase (MCAD). K364R, a folding mutation, and R256T, a catalytic-site mutation resulting in a well-folded but totally inactive proteinLinda P O'Reilly, Brage S Andresen, Paul C Engel
Pageof 5

Showing results (11-20 of 50) with videos related to

Sort By:
Pageof 5
Biochimica Et Biophysica Acta|May 26, 2009
Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stabilityXiao-Tao Wang, Paul C Engel
BMC Biotechnology|March 17, 2009
An optimised system for refolding of human glucose 6-phosphate dehydrogenaseXiao-Tao Wang, Paul C Engel
FEMS Microbiology Letters|February 26, 2008
Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coliMichael A Sharkey, Paul C Engel
FEBS Letters|May 13, 2008
Homotropic allosteric control in clostridial glutamate dehydrogenase: different mechanisms for glutamate and NAD+?Muaawia A Hamza, Paul C Engel
Proteins|May 9, 2009
Modular coenzyme specificity: a domain-swopped chimera of glutamate dehydrogenaseMichael A Sharkey, Paul C Engel
The FEBS Journal|November 12, 2013
The specificity and kinetic mechanism of branched-chain amino acid aminotransferase from Escherichia coli studied with a new improved coupled assay procedure and the enzyme's potential for biocatalysisXuejing Yu, Xingguo Wang, Paul C Engel
FEMS Microbiology Letters|February 25, 2005
Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli hostJohn B Carrigan, Suzie Coughlan, Paul C Engel
The FEBS Journal|May 14, 2011
Re-engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzymeMarina Capone, David Scanlon, Joanna Griffin, et al.
The FEBS Journal|July 25, 2007
The contribution of tryptophan residues to conformational changes in clostridial glutamate dehydrogenase--W64 and W449 as mediators of the cooperative response to glutamateMuaawia A Hamza, Stephen R Martin, Paul C Engel
The FEBS Journal|September 1, 2005
Two novel variants of human medium chain acyl-CoA dehydrogenase (MCAD). K364R, a folding mutation, and R256T, a catalytic-site mutation resulting in a well-folded but totally inactive proteinLinda P O'Reilly, Brage S Andresen, Paul C Engel
Pageof 5