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Biophysical Journal|February 1, 1996
Mechanochemical coupling in muscle: attempts to measure simultaneously shortening and ATPase rates in myofibrilsC Lionne, F Travers, T BarmanMedicine, Science, and the Law|October 1, 1994
Mental disorder amongst defendants in Liverpool Magistrates' CourtC J Brabbins, R F TraversFEBS Letters|April 9, 1991
What is the true ATPase activity of contracting myofibrils?M Houadjeto, T Barman, F TraversProceedings of the National Academy of Sciences of the United States of America|July 1, 1970
Temporal resolution of individual steps in an enzymic reaction at low temperatureP Douzou, R Sireix, F TraversFEBS Letters|January 29, 1990
Is a four-state model sufficient to describe actomyosin ATPase?C Tesi, T Barman, F TraversBiochemistry|June 28, 1988
Transient kinetics of the interaction of 1,N6-ethenoadenosine 5'-triphosphate with myosin subfragment 1 under normal and cryoenzymic conditions: a comparison with adenosine 5'-triphosphateC Tesi, F Travers, T BarmanFEBS Letters|August 15, 1988
Sulphate is a competitive inhibitor of the binding of nucleotide to myosin. A comparison with phosphateC Tesi, T Barman, F TraversThe Biochemical Journal|March 1, 1983
Evidence for the two-step binding of ATP to myosin subfragment 1 by the rapid-flow-quench methodT E Barman, D Hillaire, F TraversEuropean Journal of Biochemistry|September 1, 1980
A flow-quench apparatus for cryoenzymic studies. Application to the creatine kinase reactionT E Barman, A Brun, F TraversEuropean Journal of Biochemistry|December 1, 1981
Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experimentsJ L Markley, F Travers, C BalnyPageof 6