Thermodynamic investigation of hirudin binding to the slow and fast forms of thrombin: Evidence for folding transitions in the inhibitor and protease coupled to binding

Keyphrases

• Protease 100%
• Thrombin 100%
• Hirudin 100%
• Thermodynamic Investigation 100%
• Folding Transitions 100%
• SlowFast 33%
• Heat Capacity Change 33%
• Rapid Transition 33%
• Free Energy 16%
• Entropic Effects 16%
• Molecular Dynamics Simulation 8%
• Na + 8%
• Clot 8%
• N-terminal Domain 8%
• Protease Inhibitors 8%
• Thermodynamics 8%
• Temperature Effect 8%
• Preferential Binding 8%
• Thermodynamic Analysis 8%
• Free State 8%
• N-terminal Fragment 8%
• Difference Analysis 8%
• Absolute Value 8%
• Physiological Temperature 8%
• Fibrinogen Binding 8%
• Temperature Range 8%
• Entropy Change 8%
• Beta Chain 8%
• Preferential Interaction 8%
• Entropy Term 8%
• Surface Loops 8%
• Natural Inhibitors 8%
• Loop Shaping 8%
• Enthalpy Effects 8%
• Simulation Runs 8%
• Negative Heat Capacity 8%

Biochemistry, Genetics and Molecular Biology

• Hirudin 100%
• Protease 100%
• Thrombin 100%
• Enzyme 16%
• N-Terminus 16%
• Protease Inhibitor 8%
• Enthalpy 8%
• Fibrinogen 8%