ArticleJournal of biomolecular NMR2012
Lysine methylation strategies for characterizing protein conformations by NMR.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Quantitative Peptidomics Using Reductive Methylation of Amines.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Methyl-Induced Polarization Destabilizes the Noncovalent Interactions of N-Methylated Lysines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Analysis of βProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy.Methods in enzymology · 2019Article
- Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus onMethods in cell biology · 2019Article
- ProteinJournal of biomolecular NMR · 2017Article
- Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR.ACS chemical biology · 2016Article
- Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights.Analytical biochemistry · 2015Article
- 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Journal of biomolecular NMR · 2015Article
- Structural study of a small molecule receptor bound to dimethyllysine in lysozyme.Chemical science · 2015Article
- Review of methods to assign the nuclear magnetic resonance peaks of reductively methylated proteins.Analytical biochemistry · 2014Review
- Methods to identify the NMR resonances of the ¹³C-dimethyl N-terminal amine on reductively methylated proteins.Journal of visualized experiments : JoVE · 2013Article
- Nuclear magnetic resonance spectroscopy of the circadian clock of cyanobacteria.Integrative and comparative biology · 2013Review
- Application of reductive ¹³C-methylation of lysines to enhance the sensitivity of conventional NMR methods.Molecules (Basel, Switzerland) · 2013Article
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Authors and funding
4 authors.
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Abstract
In the presence of formaldehyde and a mild reducing agent, reductive methylation is known to achieve near complete dimethylation of protein amino groups under non-denaturing conditions, in aqueous media. Amino methylation of proteins is employed in mass spectrometric, crystallographic, and NMR studies. Where biosynthetic labeling is prohibitive, amino (13)C-methylation provides an attractive option for monitoring folding, kinetics, protein-protein and protein-DNA interactions by NMR. Here, we demonstrate two improvements over traditional (13)C-reductive methylation schemes: (1) By judicious choice of stoichiometry and pH, ε-aminos can be preferentially monomethylated. Monomethyl tags are less perturbing and generally exhibit improved resolution over dimethyllysines, and (2) By use of deuterated reducing agents and (13)C-formaldehyde, amino groups can be labeled with (13)CH(2)D tags. Use of deutero-(13)C-formaldehyde affords either (13)CHD(2), or (13)CD(3) probes depending on choice of reducing agent. Making use of (13)C-(2)H scalar couplings, we demonstrate a filtering scheme that eliminates natural abundance (13)C signal.
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