Related Experiment Video
Updated: Apr 18, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Equilibrium kinetic network of the villin headpiece in implicit solvent
1van 't Hoff Institute for Molecular Sciences, University of Amsterdam, Amsterdam, The Netherlands.
Abstract:
We applied the single-replica multiple-state transition-interface sampling method to elucidate the equilibrium kinetic network of the 35-residue-fragment (HP-35) villin headpiece in implicit water at room temperature. Starting from the native Protein Data Bank structure, nine (meta)stable states of the system were identified, from which the kinetic network was built by sampling pathways between these states. Application of transition path theory allowed analysis of the (un)folding mechanism. The resulting (un)folding rates agree well with experiments. This work demonstrates that high (un)folding barriers can now be studied.
More Related Videos
Related Concept Videos
Equilibrium Conditions for a Particle
To understand the concept of equilibrium, let us first consider the forces acting on an object. When different forces act on an object, they can...
Equations of Equilibrium in Three Dimensions
According to the vector equations of equilibrium, the vector sum of all the external forces acting on a body must...
Calculating the Equilibrium Constant
For example, gaseous nitrogen dioxide forms dinitrogen tetroxide according to this equation:
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
Introduction to Enzyme Kinetics
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...

