Influence of Detergent and Lipid Composition on Reconstituted Membrane Proteins for Structural Studies

Overview

Journal ACS Omega

Publisher American Chemical Society

Specialty Chemistry

Date 2021 Oct 4

PMID 34604620

Citations 2

Authors

Mohammed Mouhib

Andrea Benediktsdottir

Caroline Svensson Nilsson

Celestine N Chi

Affiliations

Soon will be listed here.

Abstract

Membrane proteins are frequently reconstituted in different detergents as a prerequisite to create a phospholipid environment reminiscent of their native environment. Different detergent characteristics such as their chain length and bond types could affect the structure and function of proteins. Yet, they are seldom taken into account when choosing a detergent for structural studies. Here, we explore the effect of different detergents and lipids with varying degrees of double- or single-bond composition on H-N transverse relaxation optimized spectroscopy spectra of the outer membrane protein W (OmpW). We observed changes in nuclear magnetic resonance chemical shifts for OmpW reconstituted in micelles, bicelles, and nanodiscs, depending on their detergent/lipid composition. These results suggest that a careful evaluation of detergents is necessary, so as not to jeopardize the structure and function of the protein.

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Solution nuclear magnetic resonance spectroscopy of bacterial outer membrane proteins in natively excreted vesicles using engineered Escherichia coli.

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