ArticleBiophysical journal2001
A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 78 citations in OpenAlex.
- Membrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy.Biochimica et biophysica acta. Biomembranes · 2020Article
- Contributions and Limitations of Biophysical Approaches to Study of the Interactions between Amphiphilic Molecules and the Plant Plasma Membrane.Plants (Basel, Switzerland) · 2020Review
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Journal of biomolecular NMR · 2014Article
- Membrane protein structure determination in membrana.Accounts of chemical research · 2013Article
- Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2013Review
- Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013Article
- A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles.Journal of biomolecular NMR · 2012Article
- Determining the orientation and localization of membrane-bound peptides.Current protein & peptide science · 2012Review
- AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Structure determination of membrane proteins in five easy pieces.Methods (San Diego, Calif.) · 2011Review
- Proton evolved local field solid-state nuclear magnetic resonance using Hadamard encoding: theory and application to membrane proteins.The Journal of chemical physics · 2011Article
- A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.The journal of physical chemistry. B · 2010Article
- Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes.Biophysical journal · 2009Article
- Influence of whole-body dynamics on 15N PISEMA NMR spectra of membrane proteins: a theoretical analysis.Biophysical journal · 2009Article
- Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.Molecular bioSystems · 2009Review
- Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.Biochemistry · 2008Article
- Membrane orientation of the Na,K-ATPase regulatory membrane protein CHIF determined by solid-state NMR.Magnetic resonance in chemistry : MRC · 2007Article
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1 author at 1 institution in 1 country.
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Abstract
This paper describes a simple, qualitative approach for the determination of membrane protein secondary structure and topology in lipid bilayer membranes. The approach is based on the observation of wheel-like resonance patterns observed in the NMR 1H-15N/15N polarization inversion with spin exchange at the magic angle (PISEMA) and 1H/15N heteronuclear correlation (HETCOR) spectra of membrane proteins in oriented lipid bilayers. These patterns, named Pisa wheels, have been previously shown to reflect helical wheel projections of residues that are characteristic of alpha-helices associated with membranes. This study extends the analysis of these patterns to beta-strands associated with membranes and demonstrates that, as for the case of alpha-helices, Pisa wheels are extremely sensitive to the tilt, rotation, and twist of beta-strands in the membrane. Therefore, the Pisa wheels provide a sensitive, visually accessible, qualitative index of membrane protein secondary structure and topology.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.