1-6 of 6
ANTHONY R. CLARKE
Close
Save search
Follow your search
Access your saved searches in your account
Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Articles

Molecular interactions in the RNA bacteriophage MS2

Available to Purchase
Nicola J. Stonehouse, David J. Scott, Stephanie Fonseca, James Murray, Chris Adams, Anthony R. Clarke, Karin Valegård, Roshan Golmohammadi, Sjoerd van den Worm, Lars Liljas, Peter G. Stockley
Journal: Biochemical Society Transactions
Biochem Soc Trans (1996) 24 (3): 412S.
https://doi.org/10.1042/bst024412s
Published: 01 August 1996
View articletitled, Molecular interactions in the RNA bacteriophage MS2
Open the PDF for Molecular interactions in the RNA bacteriophage MS2 in another window
Articles

Towards the construction of a universal NAD(P) + -dependent dehydrogenase: comparative and evolutionary considerations

Available to Purchase
Anthony R. Clarke, Stephen Colebrook, Antonio Cortes, David C. Emery, David J. Halsall, Keith W. Hart, Richard M. Jackson, Helen M. Wilks, J. John Holbrook
Journal: Biochemical Society Transactions
Biochem Soc Trans (1991) 19 (3): 576–581.
https://doi.org/10.1042/bst0190576
Published: 01 August 1991
View articletitled, Towards the construction of a universal NAD(P) + -dependent dehydrogenase: comparative and evolutionary considerations
Open the PDF for Towards the construction of a universal NAD(P) + -dependent dehydrogenase: comparative and evolutionary considerations in another window
Articles

Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase

Available to Purchase
TONY ATKINSON, DAVID A. BARSTOW, WILLIAM N. CHIA, ANTHONY R. CLARKE, KEITH W. HART, ADAM D. B. WALDMAN, DALE B. WIGLEY, HELEN WILKS, J. JOHN HOLBROOK
Journal: Biochemical Society Transactions
Biochem Soc Trans (1987) 15 (5): 991–993.
https://doi.org/10.1042/bst0150991
Published: 01 October 1987
View articletitled, Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase
Open the PDF for Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase in another window
Articles

Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase

Available to Purchase
ANTHONY R. CLARKE, DALE B. WIGLEY, DAVID A. BARSTOW, WILLIAM N. CHIA, ADAM D. B. WALDMAN, KEITH W. HART, TONY ATKINSON, J. JOHN HOLBROOK
Journal: Biochemical Society Transactions
Biochem Soc Trans (1987) 15 (1): 152–153.
https://doi.org/10.1042/bst0150152
Published: 01 February 1987
View articletitled, Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase
Open the PDF for Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase in another window
Articles

Low-temperature transient kinetic studies of peptide-loop movement in pig heart [Tyr(3NO 2 ) 237 ]lactate dehydrogenase

Available to Purchase
ADAM D. B. WALDMAN, ANTHONY R. CLARKE, J. JOHN HOLBROOK
Journal: Biochemical Society Transactions
Biochem Soc Trans (1985) 13 (1): 257.
https://doi.org/10.1042/bst0130257
Published: 01 February 1985
View articletitled, Low-temperature transient kinetic studies of peptide-loop movement in pig heart [Tyr(3NO 2 ) 237 ]lactate dehydrogenase
Open the PDF for Low-temperature transient kinetic studies of peptide-loop movement in pig heart [Tyr(3NO 2 ) 237 ]lactate dehydrogenase in another window
Articles

The association of apolipoprotein-CII with lipoprotein lipase in the presence and absence of a triglyceride substrate

Available to Purchase
ANTHONY R. CLARKE, MOLLIE LUSCOMBE, J. JOHN HOLBROOK
Journal: Biochemical Society Transactions
Biochem Soc Trans (1985) 13 (1): 137–138.
https://doi.org/10.1042/bst0130137
Published: 01 February 1985
View articletitled, The association of apolipoprotein-CII with lipoprotein lipase in the presence and absence of a triglyceride substrate
Open the PDF for The association of apolipoprotein-CII with lipoprotein lipase in the presence and absence of a triglyceride substrate in another window