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Updated: Jun 13, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Correlation of Solvent Interaction Analysis Signatures with Thermodynamic Properties and In Silico Calculations of
Amber R Titus1, Pedro P Madeira1,2, Vladimir N Uversky3
1Cleveland Diagnostics, 3615 Superior Ave., Cleveland, OH 44114, USA.
Abstract:
The partition behavior of single and double-point mutants of bacteriophage T4 lysozyme (T4 lysozyme) and staphylococcal nuclease A was examined in different aqueous two-phase systems (ATPSs) and studied by Solvent Interaction Analysis (SIA). Additionally, the solvent accessible surface area (SASA) of modeled mutants of both proteins was calculated. The in silico calculations and the in vitro analyses of the staphylococcal nuclease and T4 lysozyme mutants correlate, indicating that the partition analysis in ATPSs provides a valid descriptor (SIA signature) covering various protein features, such as structure, structural dynamics, and conformational stability.
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