ArticleThe journal of physical chemistry letters2011
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Article in The journal of physical chemistry letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 42 citations in OpenAlex.
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- Modest Offset Difference Internuclear Selective Transfer via Homonuclear Dipolar Coupling.The journal of physical chemistry letters · 2022Article
- Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021Article
- Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- GdJournal of biomolecular NMR · 2017Article
- Evolution of CPMAS under fast magic-angle-spinning at 100 kHz and beyond.Solid state nuclear magnetic resonance · 2015Article
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.Biochimica et biophysica acta · 2015Article
- Acceleration of natural-abundance solid-state MAS NMR measurements on bone by paramagnetic relaxation from gadolinium-DTPA.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.Journal of biomolecular NMR · 2014Article
- Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd³⁺-complexes for solid-state NMR spectroscopy.Journal of biomolecular NMR · 2014Article
- Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning.Accounts of chemical research · 2013Article
- Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.Journal of biomolecular NMR · 2012Article
- Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Journal of the American Chemical Society · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is sensitivity, due to limited quantities of labeled high-molecular-weight proteins. Here we demonstrate the incorporation of paramagnetic metal (Cu(2+)) ions, through either EDTA or a chelator lipid, into membrane protein samples for rapid data collection under fast magic-angle spinning (MAS) and low power (1)H decoupling. Spectral sensitivity of DsbB (20 kDa), an integral membrane protein, more than doubles in the same experimental time due to (1)H T(1) relaxation enhancement by Cu(2+) ions, with DsbB native fold and active site intact. This technique can be implemented to acquire multidimensional solid-state NMR spectra for chemical shift assignments and structure elucidation of large membrane proteins with small sample quantities.
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Registered trials
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.