Solution NMR investigations of integral membrane proteins: Challenges and innovations

Matthew Necelis; Connor McDermott; Meagan Belcher Dufrisne; Christopher Baryiames; Linda Columbus

doi:10.1016/j.sbi.2023.102654

Solution NMR investigations of integral membrane proteins: Challenges and innovations

Curr Opin Struct Biol. 2023 Oct:82:102654. doi: 10.1016/j.sbi.2023.102654. Epub 2023 Aug 3.

Authors

Matthew Necelis¹, Connor McDermott¹, Meagan Belcher Dufrisne¹, Christopher Baryiames¹, Linda Columbus²

Affiliations

¹ Department of Chemistry, University of Virginia, Charlottesville, VA, USA.
² Department of Chemistry, University of Virginia, Charlottesville, VA, USA. Electronic address: lc4zs@virginia.edu.

PMID: 37542910
PMCID: PMC10529709 (available on 2024-10-01)
DOI: 10.1016/j.sbi.2023.102654

Abstract

Compared to soluble protein counterparts, the understanding of membrane protein stability, solvent interactions, and function are not as well understood. Recent advancements in labeling, expression, and stabilization of membrane proteins have enabled solution nuclear magnetic resonance spectroscopy to investigate membrane protein conformational states, ligand binding, lipid interactions, stability, and folding. This review highlights these advancements and new understandings and provides examples of recent applications.

Publication types

Review
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural

MeSH terms

Magnetic Resonance Spectroscopy / methods
Membrane Proteins* / chemistry
Nuclear Magnetic Resonance, Biomolecular / methods
Protein Conformation

Substances

Membrane Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding