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Charge Interactions in a Highly Charge-Depleted Protein.

Stefan Hervø-Hansen1,2, Casper Højgaard1, Kristoffer Enøe Johansson1

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Investigating protein electrostatics, this study reveals how charged residue interactions influence protein folding. Coupled titrations form stabilized salt bridges, offering insights into protein engineering strategies.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Computational Biology

Background:

  • Electrostatic forces are crucial for protein folding and are key targets in protein engineering.
  • Studying charged residue interactions is challenging due to complex networks within proteins.

Purpose of the Study:

  • To investigate electrostatic interactions between charged residues in a simplified protein system.
  • To systematically introduce and analyze individual and paired charged/titratable residues.

Main Methods:

  • Constant pH molecular dynamics simulations
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Thermodynamic double mutant cycles

Main Results:

  • Partial burial of surface charges shifts pKa values, enabling aspartate titration near neutral pH.
  • Interactions between residue pairs are context-dependent, ranging from no preferential interaction to stabilized salt bridges via coupled titration.

Conclusions:

  • Experimental and simulation results show good agreement, providing mechanistic understanding of electrostatic interactions.
  • The findings offer detailed insights into how charged residues influence protein structure and function, aiding protein engineering efforts.