Doubly spin-labeled nanodiscs to improve structural determination of membrane proteins by ESR
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Summary
The use of nanodiscs (NDs) are reported to improve the distance resolution of pulsed dipolar spectroscopy by increasing the overall amplitude of dipolar signals, leading to a critical enhancement of thedistance resolution.
- Type
- article
- Published
- 2019-03-15
- Cited by
- 6
- References
- 29
- Access
- Open access
- OpenAlex
- https://openalex.org/W2924141382
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:109537985
Keywords
Nanodisc, Membrane, Chemistry, Resolution (logic), Homogeneity (statistics)
References
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- Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR.
- Visualization of distance distribution from pulsed double electron-electron resonance data
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- Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin
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- Protonation-dependent conformational dynamics of the multidrug transporter EmrE
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- Lipids modulate the conformational dynamics of a secondary multidrug transporter
Cited by
- Identifying Protein Conformational Dynamics Using Spin-label ESR.
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins
- Anti-apoptotic BCL-2 regulation by changes in dynamics of its long unstructured loop
- Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques
- Nanodisc Lipids Exhibit Singular Behaviors Implying Critical Phenomena.
- A gating mechanism of the BsYetJ calcium channel revealed in an endoplasmic reticulum lipid environment.
- An Inactivation Gate of the BsYetJ Calcium Channel That Becomes Functional in the Endoplasmic Reticulum Environment
- The Inactivation Gates of BsYetJ Calcium Channel Revealed in the Endoplasmic Reticulum Environment
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