Multi-site fluorescence energy transfer shows Ca2+-induced tropomyosin movement in reconstituted skeletal muscle thin filaments

Fluorescence energy transfer studies of the tropomyosin movement in reconstituted skeletal muscle thin filaments. Biophysical Journal 76(1 PART 2): A154, 1999

Ca(2+)- and S1-induced movement of troponin T on reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy. Journal of Biochemistry 132(1): 93-102, 2002

Ca2+S1-Induced Movement of Troponin T on Reconstituted Skeletal Muscle Thin Filaments Observed by Fluorescence Energy Transfer Spectroscopy. Journal of Biochemistry 132(1): 93-102, 2002

Ca(2+)-induced movement of tropomyosin in skeletal muscle thin filaments observed by multi-site FRET. Biophysical Journal 82(3): 1524-1536, 2002

Fluorescence resonance energy transfer between points on tropomyosin and actin in skeletal muscle thin filaments: does tropomyosin move?. Journal of Biochemistry 123(6): 1104-1111, 1998

Ca2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: structural evidence for three States of thin filament. Journal of Biochemistry 131(3): 407-418, 2002

Ca2+- and Sl-Induced Conformational Changes of Reconstituted Skeletal Muscle Thin Filaments Observed by Fluorescence Energy Transfer Spectroscopy: Structural Evidence for Three States of Thin Filament. Journal of Biochemistry 131(3): 407-418, 2002

Fluorescence resonance energy transfer between points on actin and the C-terminal region of tropomyosin in skeletal muscle thin filaments. Journal of Biochemistry 136(1): 39-47, 2004

Kinetics of structural changes of reconstituted skeletal muscle thin filaments observed by fluorescence resonance energy transfer. Journal of Biological Chemistry 268(10): 7101-7106, 1993

Excitation energy transfer studies of the proximity between tropomyosin and actin in reconstituted skeletal muscle thin filaments. Computer simulation study on the extent of energy transfer from a single Tm-bound donor to multiple actin-bound acceptors. Biochemistry 22(13): 3059-3066, 1983

The rates of switching movement of troponin T between three states of skeletal muscle thin filaments determined by fluorescence resonance energy transfer. Journal of Biological Chemistry 280(4): 2613-2619, 2004

Excimer fluorescence of pyrenyliodoacetamide-labeled tropomyosin: a probe of the state of tropomyosin in reconstituted muscle thin filaments. Biochemistry 29(5): 1160-1166, 1990

Ca2+-induced distance change between points on actin and troponin in skeletal muscle thin filaments estimated by fluorescence energy transfer spectroscopy. Journal of Biochemistry 123(2): 324-331, 1998

Fluorescence probe studies of the state of tropomyosin in reconstituted muscle thin filaments. Biochemistry 26(16): 4922-4925, 1987

Excitation energy transfer studies of the proximity between tropo myosin and actin in reconstituted skeletal muscle thin filaments. Biochemistry 22(13): 3059-3066, 1983