The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR
Abstract
Membrane proteins remain difficult to study by traditional methods. Magic angle spinning solid-state NMR (MAS SSNMR) methods present an important approach for studying membrane proteins of moderate size. Emerging MAS SSNMR methods are based on extensive assignments of the nuclei as a basis for structure determination and characterization of function. These methods have already been used to characterize fibrils and globular proteins and are being increasingly used to study membrane proteins embedded in lipids. This review highlights recent applications to intrinsic membrane proteins and summarizes recent technical advances that will enable these methods to be utilized for more complex membrane protein systems in the near future.
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Cites
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Nuclear Magnetic Resonance Spectra from a Crystal rotated at High Speed
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Metadata
- Authors
- McDermott, A.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2009-06-01
- Volume
- 38
- Issue
- 1
- Pages
- 385-403
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2132954592
- Cited by
- 342
- References
- 95
- FWCI
- 2.05
- Type
- journal article
- Language
- en
- Open access
- closed
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- McDermott, A. (2009). Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR. Annual Review of Biophysics. https://doi.org/10.1146/annurev.biophys.050708.133719
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