Cation-π Interactions and their Functional Roles in Membrane Proteins

Daniel T Infield; Ali Rasouli; Grace D Galles; Christophe Chipot; Emad Tajkhorshid; Christopher A Ahern

doi:10.1016/j.jmb.2021.167035

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Cation-π Interactions and their Functional Roles in Membrane Proteins

Journal article

Peer reviewed

Cation-π Interactions and their Functional Roles in Membrane Proteins

Daniel T Infield, Ali Rasouli, Grace D Galles, Christophe Chipot, Emad Tajkhorshid and Christopher A Ahern

Journal of molecular biology, Vol.433(17), 167035

08/20/2021

DOI: 10.1016/j.jmb.2021.167035

PMCID: PMC8338773

PMID: 33957146

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https://www.ncbi.nlm.nih.gov/pmc/articles/8338773View

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Abstract

Cation-π interactions arise as a result of strong attractive forces between positively charged entities and the π-electron cloud of aromatic groups. The physicochemical characteristics of cation-π interactions are particularly well-suited to the dual hydrophobic/hydrophilic environment of membrane proteins. As high-resolution structural data of membrane proteins bring molecular features into increasingly sharper view, cation-π interactions are gaining traction as essential contributors to membrane protein chemistry, function, and pharmacology. Here we review the physicochemical properties of cation-π interactions and present several prominent examples which demonstrate significant roles for this specialized biological chemistry.

Computational Chemistry

Ion Channels

GPCR

genetic code expansion

cation-pi interactions

Details

Title: Subtitle: Cation-π Interactions and their Functional Roles in Membrane Proteins
Creators: Daniel T Infield - Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA
Ali Rasouli - Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Grace D Galles - Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA
Christophe Chipot - Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Emad Tajkhorshid - Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Christopher A Ahern - Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA
Resource Type: Journal article
Publication Details: Journal of molecular biology, Vol.433(17), 167035
DOI: 10.1016/j.jmb.2021.167035
PMID: 33957146
PMCID: PMC8338773
NLM abbreviation: J Mol Biol
ISSN: 0022-2836
eISSN: 1089-8638
Publisher: Elsevier Ltd
Language: English
Electronic publication date: 05/03/2021
Date published: 08/20/2021
Academic Unit: Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984077781902771

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