Structural Rearrangements of Membrane Proteins Probed by Water-Edited Solid-State NMR Spectroscopy
Abstract
We show that water-edited solid-state NMR spectroscopy allows for probing global protein conformation and residue-specific solvent accessibility in a lipid bilayer environment. The transfer dynamics can be well described by a general time constant, irrespective of protein topology and lipid environment. This approach was used to follow structural changes in response to protein function in the chimeric potassium channel KcsA-Kv1.3. Data obtained as a function of pH link earlier biochemical data to changes in protein structure in a functional bilayer setting.
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The relative intensity ratio between the water-edited spectrum and the control spectrum reflects the extent of hydration of cell wall samples.
“The relative intensity ratio between the water-edited spectrum and the control spectrum was quantified for all cell wall samples to reflect the extent of hydration.”
From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [119]
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Molecular architecture of fungal cell walls revealed by solid-state NMR
Kang, X., Kirui, A., Muszyński, A., Widanage, M. C. D., Chen, A., Azadi, P., Wang, P., Mentink-Vigier, F., & Wang, T. (2018) · Nature Communications · doi:10.1038/s41467-018-05199-0 · Cited by 356 · see citing works
Dickwella Widanage, M. C., Singh, K., Li, J., Yarava, J. R., Scott, F. J., Xu, Y., Gow, N. A. R., Mentink-Vigier, F., Wang, P., Lamoth, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61678-1 · Cited by 51 · see citing works
- Authors
- Ader, C., Schneider, R., Seidel, K., Etzkorn, M., Becker, S., & Baldus, M.
- Affiliations
- Utrecht University (NL)
- Corresponding author
- Baldus, Marc
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-12-08
- Volume
- 131
- Issue
- 1
- Pages
- 170-176
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2065145701
- Cited by
- 124
- References
- 0
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 10 · 2023: 6 · 2022: 3 · 2021: 8 · 2020: 2 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 10 · 2013: 11 · 2012: 7
- FWCI
- 3.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- membrane protein structure, lipid bilayers, protein conformation, protein function
- MeSH terms
- Phospholamban, Bacterial Proteins, Calcium-Binding Proteins, Lipid Bilayers, Models, Chemical, Models, Molecular, Water, Potassium Channels, Nuclear Magnetic Resonance, Biomolecular, Halorhodopsins, Sensory Rhodopsins
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