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Updated: Sep 13, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein
Joel Mieres-Perez1, Yasser Almeida-Hernandez1, Wolfram Sander2
1Chair of Computational Bioengineering, Department of Biochemical and Chemical Engineering, TU Dortmund University, 44227 Dortmund, Germany.
Abstract:
Intermolecular interactions play a key role in determining and tuning the structure and function of proteins. Following a simplified conventional scheme, molecular interactions are often classified as strong (long-range), typically driven by ionic contacts and salt bridges, or as weak (short-range), such as hydrophobic interactions. The reality is more complex, with classical strong interactions having weak contributions and vice versa. The interaction network regulating the properties of biomolecular systems such as proteins and their media goes beyond a single sort of contribution, and instead it is characterized by the interplay between several forces of diverse nature. In this review, we discuss, via selected examples, state of the art methodologies and applications of computational techniques to explore the role of intermolecular interactions, with emphasis on solvent effects on protein folding, enzymatic activity, and protein-peptide binding.
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