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Biochemistry|October 8, 1997
Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivitiesK Polosukhina, S HighsmithBiochemistry|January 13, 1987
Spatial organization of CaATPase molecules in sarcoplasmic reticulum vesiclesS Highsmith, J A CohenBiochemistry|January 21, 1992
Electrostatic changes at the actomyosin-subfragment 1 interface during force-generating reactionsS Highsmith, A J MurphyBiochimica Et Biophysica Acta|September 3, 1993
The ATP-induced myosin subfragment-1 fluorescence intensity increase is due to one tryptophanS J Papp, S HighsmithThe Journal of Biological Chemistry|December 10, 1984
Nd3+ and Co2+ binding to sarcoplasmic reticulum CaATPase. An estimation of the distance from the ATP binding site to the high-affinity calcium binding sitesS Highsmith, A J MurphyOrganizational Behavior and Human Performance|November 7, 1982
Critical job events, acute stress, and strain: a multiple interrupted time seriesD EdenBiophysical Chemistry|March 27, 1997
Skeletal muscle myosin subfragment 1 dimersK Claire, R Pecora, S HighsmithProtein Science : a Publication of the Protein Society|September 24, 1999
Predicting allosteric switches in myosinsK Kirshenbaum, M Young, S HighsmithBiophysical Journal|September 1, 1993
Cross-linking myosin subfragment 1 Cys-697 and Cys-707 modifies ATP and actin binding site interactionsK Kirshenbaum, S Papp, S HighsmithBiochimica Et Biophysica Acta|July 11, 1985
High-affinity and low-affinity vanadate binding to sarcoplasmic reticulum Ca2+-ATPase labeled with fluorescein isothiocyanateS Highsmith, D Barker, D J ScalesPageof 11