Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy.

ABSTRACT: The structural characterization of membrane proteins within the cellular membrane environment is critical for understanding the molecular mechanism in their native functional context. However, conducting residue site-specific structural analysis of membrane proteins in native membranes by solid-state NMR faces challenges due to poor spectral sensitivity and serious interference from background protein signals. In this study, we present a new protocol that combines various strategies for cellular membrane sample preparations, enabling us to reveal the secondary structure of the mechanosensitive channel of large conductance from Methanosarcina acetivorans (MaMscL) in Escherichia coli inner membranes. Our findings demonstrate the feasibility of achieving complete resonanc

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC10751765 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature