ReviewAdvances in experimental medicine and biology2012
Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.
Review in Advances in experimental medicine and biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
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- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Nuclear spin effects in biological processes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Improved spectral resolution of [Journal of biomolecular NMR · 2023Article
- Great Offset Difference Internuclear Selective Transfer.The journal of physical chemistry letters · 2023Article
- Determination of protein conformation and orientation at buried solid/liquid interfaces.Chemical science · 2023Article
- A method for selectiveProtein science : a publication of the Protein Society · 2022Article
- Modest Offset Difference Internuclear Selective Transfer via Homonuclear Dipolar Coupling.The journal of physical chemistry letters · 2022Article
- NMR resonance assignments of human Atg3 in aqueous solution and bicelles.Biomolecular NMR assignments · 2021Article
- Met125 is essential for maintaining the structural integrity of calmodulin's C-terminal domain.Scientific reports · 2020Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- NMR as a "Gold Standard" Method in Drug Design and Discovery.Molecules (Basel, Switzerland) · 2020Review
- Lipid-nanodiscs formed by paramagnetic metal chelated polymer for fast NMR data acquisition.Biochimica et biophysica acta. Biomembranes · 2020Article
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
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5 authors.
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Abstract
In this chapter, we summarize the isotopic labeling strategies used to obtain high-quality solution and solid-state NMR spectra of biological samples, with emphasis on integral membrane proteins (IMPs). While solution NMR is used to study IMPs under fast tumbling conditions, such as in the presence of detergent micelles or isotropic bicelles, solid-state NMR is used to study the structure and orientation of IMPs in lipid vesicles and bilayers. In spite of the tremendous progress in biomolecular NMR spectroscopy, the homogeneity and overall quality of the sample is still a substantial obstacle to overcome. Isotopic labeling is a major avenue to simplify overlapped spectra by either diluting the NMR active nuclei or allowing the resonances to be separated in multiple dimensions. In the following we will discuss isotopic labeling approaches that have been successfully used in the study of IMPs by solution and solid-state NMR spectroscopy.
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