ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2012
Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- Effects of deuteration on solid-state NMR spectra of single peptide crystals and oriented protein samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.Journal of biomolecular NMR · 2014Article
- Mechanism of dilute-spin-exchange in solid-state NMR.The Journal of chemical physics · 2014Article
- Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Journal of biomolecular NMR · 2014Article
- Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers.The Journal of chemical physics · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We demonstrate (1)H amide resonance line widths <300 Hz in (1)H/(15)N heteronuclear correlation (HETCOR) spectra of membrane proteins in aligned phospholipid bilayers. This represents a substantial improvement over typically observed line widths of ∼1 kHz. Furthermore, in a proton detected local field (PDLF) version of the experiment that measures heteronuclear dipolar couplings, line widths <130 Hz are observed. This dramatic line narrowing of (1)H amide resonances enables many more individual signals to be resolved and assigned from uniformly (15)N labeled membrane proteins in phospholipid bilayers under physiological conditions of temperature and pH. Finding that the decrease in line widths occurs only for membrane proteins that undergo fast rotational diffusion around the bilayer normal, but not immobile molecules, such as peptide single crystals, identifies a potential new direction for pulse sequence development that includes overall molecular dynamics in their design.
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