Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
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Membrane proteins mediate processes that are fundamental for the flourishing of biological cells. Membrane-embedded transporters move ions and larger solutes across membranes; receptors mediate communication between the cell and its environment and membrane-embedded enzymes catalyze chemical reactions. Understanding these mechanisms of action requires knowledge of how the proteins couple to their fluid, hydrated lipid membrane environment. We present here current studies in computational and experimental membrane protein biophysics, and show how they address outstanding challenges in understanding the complex environmental effects on the structure, function, and dynamics of membrane proteins.
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Dynamic interconversion between multiple conformations underpins the functions of integral membrane proteins in all domains of life.
“Dynamic interconversion between multiple conformations underpins the functions of integral membrane proteins in all domains of life (Campbell et al., 2016; Cournia et al., 2015; Shaw et al., 2010; Boehr et al., 2009).”
From Sampling alternative conformational states of transporters and receptors with AlphaFold2 (2022) · cites this paper as Cournia et al., 2015
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- Authors
- Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., Friedman, R., Gkeka, P., Hege, H.-C., Hénin, J., Kasimova, M. A., Kolocouris, A., Klein, M. L., Khalid, S., Lemieux, M. J., Lindow, N., Roy, M., Selent, J., Tarek, M., Tofoleanu, F., Vanni, S., Urban, S., Wales, D. J., Smith, J. C., & Bondar, A.-N.
- Affiliations
- Academy of Athens (GR)
- RMIT University (AU)
- University of California, Irvine (US)
- Centre National de la Recherche Scientifique (FR)
- Zuse Institute Berlin (DE)
- Rutgers, The State University of New Jersey (US)
- University College Dublin (IE)
- Temple University (US)
- Linnaeus University (SE)
- Lomonosov Moscow State University (RU)
- National and Kapodistrian University of Athens (GR)
- University of Southampton (GB)
- University of Alberta (CA)
- Universitat Pompeu Fabra (ES)
- University of Cambridge (GB)
- Oak Ridge National Laboratory (US)
- Freie Universität Berlin (DE)
- Corresponding author
- Cournia, Zoe
- Smith, Jeremy C.
- Bondar, Ana-Nicoleta
- ORCID
- Cournia, Zoe
- Allen, Toby W.
- Andricioaei, Ioan
- Antonny, Bruno
- Baum, Daniel
- Brannigan, Grace
- Buchete, Nicolae-Viorel
- Delemotte, Lucie
- Friedman, Ran
- Gkeka, Paraskevi
- Hege, Hans-Christian
- Hénin, Jérôme
- Kasimova, Marina A.
- Kolocouris, Antonios
- Klein, Michael L.
- Khalid, Syma
- Lemieux, M. Joanne
- Lindow, Norbert
- Selent, Jana
- Tarek, Mounir
- Tofoleanu, Florentina
- Vanni, Stefano
- Wales, David J.
- Smith, Jeremy C.
- Bondar, Ana-Nicoleta
- Venue
- The Journal of Membrane Biology
- Published
- 2015-06-11
- Volume
- 248
- Issue
- 4
- Pages
- 611-640
- ISSN
- 0022-2631 (ISSN-L)
- 1432-1424
- PMC
- PMC4515176
- OpenAlex
- W2103496068
- Cited by
- 235
- References
- 282
- Citations by year
- 2026: 11 · 2025: 23 · 2024: 36 · 2023: 37 · 2022: 18 · 2021: 28 · 2020: 27 · 2019: 15 · 2018: 18 · 2017: 12 · 2016: 10
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- The Journal of Membrane Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RECERCAT (Consorci de Serveis Universitaris de Catalunya) (acceptedVersion, other-oa)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- HAL (submittedVersion, public-domain)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Figshare (submittedVersion)
- Repositori digital de la UPF (Universitat Pompeu Fabra) (submittedVersion)
- Funders
- National Science Foundation (1052477, RC2GM093307, 0840513)
- National Institutes of Health
- University of California, Irvine
- Australian Research Council (DP120103548)
- European Regional Development Fund
- National Cancer Institute (2010-1)
- National Institute of General Medical Sciences (P01GM55876-14A1, P01GM055876, RC2GM093307)
- Division of Chemistry (CHE-0840513)
- FP7 Ideas: European Research Council (268888)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- membrane proteins, membrane protein structure, membrane protein dynamics, membrane protein function, membrane transporters, cell surface receptors, protein-lipid interactions, computational biophysics
- MeSH terms
- Animals, Humans, Models, Biological, Models, Chemical, Structure-Activity Relationship, Protein Structure, Tertiary, Membrane Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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