Intrinsic tryptophan fluorescence identifies specific conformational changes at the actomyosin interface upon actin binding and ADP release

Keyphrases

• Conformational Change 100%
• Actin Binding 100%
• ADP Release 100%
• Actomyosin 100%
• A-site 100%
• Intrinsic Tryptophan Fluorescence 100%
• Actin 66%
• Dimethyl 66%
• Quantum Yield 66%
• O-nitrobenzyl 66%
• Sulfonium 66%
• Bromide Oxidation 66%
• Tryptophan 33%
• Essential Light Chain 33%
• Myosin 33%
• Motor Domain 33%
• Smooth muscle Myosin 33%
• Myosin Motor 33%
• Actin-activated ATPase 33%
• Structural Features 33%
• Emission Peak 33%
• Steady-state Fluorescence 33%
• Helix-loop-helix 33%
• Binding Properties 33%
• Fluorescence Property 33%
• Myopathy 33%
• Crystallographic Data 33%
• Actomyosin Complex 33%
• Acrylamide 33%
• Bimolecular Quenching Constant 33%
• Binding Interface 33%

Biochemistry, Genetics and Molecular Biology

• Conformational Change 100%
• Actin 100%
• Tryptophan 100%
• Adenosine Diphosphate 100%
• Myosin ATPase 100%
• Conformation 50%
• Alpha Oxidation 33%
• Quantum Yield 33%
• Wild Type 16%
• Steady State 16%
• ATPase 16%
• Nucleotide 16%
• Light Chain 16%