Assessment of the Components of the Electrostatic Potential of Proteins in Solution: Comparing Experiment and Theory

Chuanying Chen, Binhan Yu, Razie Yousefi, Junji Iwahara, B. Montgomery Pettitt

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

In this work, the components of the protein electrostatic potentials in solution are analyzed with NMR paramagnetic relaxation enhancement experiments and compared with continuum solution theory, and multiscale simulations. To determine the contributions of the solution components, we analyze them at different ionic strengths from 0 to 745 mM. A theoretical approximation allows the determination of the electrostatic potential at a given proton without reference to the protein structure given the ratio of paramagnetic relaxation enhancements rates between a cationic and an anionic probe. The results derived from simulations show good agreement with experiment and simple continuum solvent theory for many of the residues. A discrepancy including a switch of sign of the electrostatic potential was observed for particular residues. By considering the components of the potential, we found the discrepancy is mainly caused by angular correlations of the probe molecules with these residues. The correction for the correlations allows a more accurate analysis of the experiments determining the electrostatic potential of proteins in solution.

Original languageEnglish (US)
Pages (from-to)4543-4554
Number of pages12
JournalJournal of Physical Chemistry B
Volume126
Issue number24
DOIs
StatePublished - Jun 23 2022
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

Fingerprint

Dive into the research topics of 'Assessment of the Components of the Electrostatic Potential of Proteins in Solution: Comparing Experiment and Theory'. Together they form a unique fingerprint.

Cite this