Probing Residue-Specific Water–Protein Interactions in Oriented Lipid Membranes via Solid-State NMR Spectroscopy
Author:
Affiliation:
1. Department of Biochemistry, Molecular Biology, and Biophysics and ‡Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.6b08282
Reference63 articles.
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4. NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
5. Limiting an Antimicrobial Peptide to the Lipid−Water Interface Enhances Its Bacterial Membrane Selectivity: A Case Study of MSI-367
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1. Detecting water-protein chemical exchange in membrane-bound proteins/peptides by solid-state NMR spectroscopy;Magnetic Resonance Letters;2021-11
2. Hydrophobic Gate of Mechanosensitive Channel of Large Conductance in Lipid Bilayers Revealed by Solid-State NMR Spectroscopy;The Journal of Physical Chemistry B;2021-03-09
3. Magnetically-orientable Tween-based model membranes for NMR studies of proteins;Biochimica et Biophysica Acta (BBA) - Biomembranes;2020-10
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