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R Cardinaud

Showing results (21-30 of 33) with videos related to

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Journal of Medicinal Chemistry|May 1, 1970
Irreversible enzyme inibitiors. CLXXII. Proteolytic enzymes. XVI. Covalent bonding of the sulfonyl fluoride group to serine outside the active site of alpha-chymotrypsin by exo-type active-site directed irreversible inhibitorsR Cardinaud, B R Baker
European Biophysics Journal : EBJ|January 1, 1991
Flexibility of myosin in pyrophosphate and NaCl solutions. An electric birefringence studyR Cardinaud, J C Bernengo
Biophysical Journal|November 1, 1985
Electric birefringence study of rabbit skeletal myosin subfragments HMM, LMM, and rod in solutionR Cardinaud, J C Bernengo
Biochimica Et Biophysica Acta|March 1, 1990
Conformational calculations on the Ala14-Pro27 LC1 segment of rabbit skeletal myosinE Abillon, L Bremier, R Cardinaud
Biochemical and Biophysical Research Communications|February 9, 1976
Separation of two HMM-S1 species from white muscle myosinR Cardinaud, F Guillain, A Bluzat
Biochemical and Biophysical Research Communications|June 8, 1973
Heterogeneity of subfragment-1 preparations from myofibril digestion by trypsinR Cardinaud, E Dassin, F Pelletier
Thrombosis and Haemostasis|December 30, 1983
75Se-seleno-methionine-actin as a probe for determination of platelet production rateR Cardinaud, E Dassin, J Bourebia
FEBS Letters|August 7, 1995
Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymesJ M Burgat, C Ghelis, R Cardinaud
European Journal of Biochemistry|August 15, 1993
The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformationA Roulet, J M Burgat, R Cardinaud
Biochimie|December 1, 1992
Refined conditions for selective modifications of rabbit skeletal myosin light chainsJ M Burgat, A Roulet, R Cardinaud
Pageof 4

Showing results (21-30 of 33) with videos related to

Sort By:
Pageof 4
Journal of Medicinal Chemistry|May 1, 1970
Irreversible enzyme inibitiors. CLXXII. Proteolytic enzymes. XVI. Covalent bonding of the sulfonyl fluoride group to serine outside the active site of alpha-chymotrypsin by exo-type active-site directed irreversible inhibitorsR Cardinaud, B R Baker
European Biophysics Journal : EBJ|January 1, 1991
Flexibility of myosin in pyrophosphate and NaCl solutions. An electric birefringence studyR Cardinaud, J C Bernengo
Biophysical Journal|November 1, 1985
Electric birefringence study of rabbit skeletal myosin subfragments HMM, LMM, and rod in solutionR Cardinaud, J C Bernengo
Biochimica Et Biophysica Acta|March 1, 1990
Conformational calculations on the Ala14-Pro27 LC1 segment of rabbit skeletal myosinE Abillon, L Bremier, R Cardinaud
Biochemical and Biophysical Research Communications|February 9, 1976
Separation of two HMM-S1 species from white muscle myosinR Cardinaud, F Guillain, A Bluzat
Biochemical and Biophysical Research Communications|June 8, 1973
Heterogeneity of subfragment-1 preparations from myofibril digestion by trypsinR Cardinaud, E Dassin, F Pelletier
Thrombosis and Haemostasis|December 30, 1983
75Se-seleno-methionine-actin as a probe for determination of platelet production rateR Cardinaud, E Dassin, J Bourebia
FEBS Letters|August 7, 1995
Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymesJ M Burgat, C Ghelis, R Cardinaud
European Journal of Biochemistry|August 15, 1993
The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformationA Roulet, J M Burgat, R Cardinaud
Biochimie|December 1, 1992
Refined conditions for selective modifications of rabbit skeletal myosin light chainsJ M Burgat, A Roulet, R Cardinaud
Pageof 4