Nuclear magnetic resonance of membrane proteins-Advances and opportunities. Curr Opin Struct Biol 2026 Jun;98:103284
Date
05/14/2026Pubmed ID
42127748Pubmed Central ID
PMC13524125DOI
10.1016/j.sbi.2026.103284Scopus ID
2-s2.0-105039288325 (requires institutional sign-in at Scopus site)Abstract
Nuclear magnetic resonance (NMR) has a long history of addressing mechanistic questions in membrane biology. Its unique capabilities include the non-perturbing nature of isotope labels, the ability of NMR signals to provide atomic-level structural and dynamic information in complex samples, including living systems, and the ability to detect very weak binding through chemical shift changes. Solution and solid-state NMR methods are highly complementary and enable a wide range of biomolecular complexity and dynamic timescales to be analyzed. Here we describe recent advances that push the envelope of current technology and offer new opportunities for targeting membrane protein assemblies to gain fundamental human health insights.
Author List
Shin K, Gopinath T, Marassi FMAuthors
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinKyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
Gopinath Tata PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnimalsHumans
Membrane Proteins
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
