Loop L5 assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5: A transient and time-resolved fluorescence study

Keyphrases

• Molecular Motor 100%
• Time-resolved Fluorescence 100%
• Microtubule Binding 100%
• Fluorescence Studies 100%
• ATPase Cycle 100%
• Mitotic Kinesin 100%
• Mitosis 50%
• Microtubules 50%
• Bound States 50%
• State-resolved 50%
• Steady State 50%
• Local Environment 50%
• Helix 50%
• Substrate Binding 50%
• Structural Domains 50%
• Stem-loop 50%
• Fluorescent Probe 50%
• Product Release 50%
• Kinesin Superfamily 50%
• Nucleotide Binding 50%
• Bipolar Spindle 50%
• Transient Kinetics 50%
• Static Image 50%
• Nucleotide State 50%
• Cryo-EM Reconstruction 50%
• Steady Time 50%
• Opposing Forces 50%
• Reversible Interaction 50%
• Segmental Mobility 50%
• Distribution Shift 50%
• Time-resolved Methods 50%
• Equilibrium Mixture 50%
• Environment Mobility 50%

Biochemistry, Genetics and Molecular Biology

• Kinesin 100%
• ATPase 100%
• Conformation 66%
• Nucleotide 66%
• Reconstruction 33%
• Fluorescent Probes 33%
• Steady State 33%
• Stem-Loop 33%
• Cryoelectron Microscopy 33%
• Mitosis 33%

Neuroscience

• Microtubules 100%
• Adenosine Triphosphatase 100%
• Kinesin 100%
• Fluorescent Dye 33%
• Stem-Loop 33%
• Cryo-Electron Microscopy 33%
• Mitosis 33%