Protein Electrostatics Investigated through Paramagnetic NMR for Nonpolar Groups

Binhan Yu, Channing C. Pletka, Junji Iwahara

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Experimental validation of theoretical models for protein electrostatics remains rare. Recently, we have developed a paramagnetic NMR-based method for de novo determination of effective near-surface electrostatic potentials, which allows for straightforward examination of electrostatic models for biomolecules. In the current work, we expand this method and demonstrate that effective near-surface electrostatic potentials can readily be determined from 1H paramagnetic relaxation enhancement (PRE) data for protein CαH and CH3groups. The experimental data were compared with those predicted from the Poisson-Boltzmann theory. The impact of structural dynamics on the effective near-surface electrostatic potentials was also assessed. The agreement between the experimental and theoretical data was particularly good for methyl 1H nuclei. Compared to the conventional pKa-based validation, our paramagnetic NMR-based approach can provide a far larger number of experimental data that can directly be used to examine the validity of theoretical electrostatic models for proteins.

Original languageEnglish (US)
Pages (from-to)2196-2202
Number of pages7
JournalJournal of Physical Chemistry B
Volume126
Issue number11
DOIs
StatePublished - Mar 24 2022

ASJC Scopus subject areas

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

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