Mechanism of substrate translocation by a ring-shaped ATPase motor at millisecond resolution

Keyphrases

• All-atom Molecular Dynamics Simulation 33%
• Allosteric Site 33%
• Atomic Level 33%
• ATP Hydrolysis 33%
• ATPase Motor 100%
• Cellular Processes 33%
• Chemical Energy 33%
• Conformational States 33%
• Conformational Transition 33%
• Effective Approach 33%
• Free Energy Profile 33%
• Generative Process 33%
• Genome Replication 33%
• Hexameric ATPase 33%
• Hydrolysis 66%
• Hydrolysis Products 66%
• Intermediate State 33%
• K326 33%
• Mechanical Force 33%
• Millisecond Resolution 100%
• Motor Action 33%
• Multimeric Enzymes 33%
• Path Sampling 33%
• Population Shift 33%
• Product Release 33%
• Product State 33%
• Protein Degradation 33%
• Relative Rotation 33%
• Relative Translation 33%
• Replication Protein A 33%
• Ring-like Structures 100%
• RNA Substrates 33%
• Sampling Methods 33%
• Side Chain 33%
• Single Guide RNA (sgRNA) 33%
• Substrate Translocation 100%
• Transcription Termination Factor 33%
• Translocated 100%

Biochemistry, Genetics and Molecular Biology

• Adenosine Diphosphate 20%
• Adenosine Triphosphate 20%
• Allosteric Site 20%
• ATPase 100%
• Conformation 20%
• Conformational Change 20%
• Dynamics 20%
• Enzymatic Hydrolysis 100%
• Enzyme 20%
• Messenger RNA 20%
• Motion 20%
• Protein Catabolism 20%
• RNA 40%
• Termination Factor 20%
• Transcription 20%
• Transcription Termination 20%