Correlation of Solvent Interaction Analysis Signatures with Thermodynamic Properties and In Silico Calculations of the Structural Effects of Point Mutations in Two Proteins

Int J Mol Sci. 2024 Sep 6;25(17):9652. doi: 10.3390/ijms25179652.

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.

Keywords: aqueous two-phase system; bacteriophage T4 lysozyme; conformational stability; protein partitioning; solvent interaction analysis; staphylococcal nuclease A; structural signature.

MeSH terms

  • Bacteriophage T4* / enzymology
  • Bacteriophage T4* / genetics
  • Computer Simulation
  • Micrococcal Nuclease* / chemistry
  • Micrococcal Nuclease* / genetics
  • Micrococcal Nuclease* / metabolism
  • Models, Molecular
  • Muramidase* / chemistry
  • Muramidase* / genetics
  • Muramidase* / metabolism
  • Point Mutation*
  • Protein Conformation
  • Solvents* / chemistry
  • Thermodynamics*
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / metabolism

Substances

  • Muramidase
  • Solvents
  • Micrococcal Nuclease
  • Viral Proteins

Grants and funding

This research received no external funding.