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Probing Slow Time Scale Dynamics at Methyl-Containing Side Chains in Proteins by Relaxation Dispersion NMR Measurements: Application to Methionine Residues in a Cavity Mutant of T4 Lysozyme
Abstract
A relaxation dispersion-based NMR experiment is presented for the measurement and quantitation of micros-ms dynamic processes at methyl side-chain positions in proteins. The experiment measures the exchange contribution to the 13C line widths of methyl groups using a constant-time CPMG scheme. The effects of cross-correlated spin relaxation between dipole-dipole and dipole-CSA interactions as well as the effects of scalar coupling responsible for mixing of magnetization modes during the course of the experiment have been investigated in detail both theoretically and through simulations. It is shown that the complex relaxation properties of the methyl spin system do not complicate extraction of accurate exchange parameters as long as care is taken to ensure that appropriate magnetization modes are interchanged in the middle of the constant-time CPMG period. An application involving the measurement of relaxation dispersion profiles of methionine residues in a Leu99Ala substitution of T4 lysozyme is presented. All of the methionine residues are sensitive to an exchange event with a rate on the order of 1200 s(-1) at 20 degrees C that may be linked to a process in which hydrophobic ligands are able to rapidly bind to the cavity that is present in this mutant.
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Citations
Cites
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
Cited by
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Korzhnev, D. M., & Kay, L. E. (2008) · Accounts of Chemical Research · doi:10.1021/ar700189y · Cited by 268
Self-citationBrath, U., Akke, M., Yang, D., Kay, L. E., & Mulder, F. A. A. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0570279 · Cited by 57
Metadata
- Authors
- Skrynnikov, N. R., Mulder, F. A. A., Hon, B., Dahlquist, F. W., & Kay, L. E.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-04-19
- Volume
- 123
- Issue
- 19
- Pages
- 4556-4566
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1965676565
- Cited by
- 186
- References
- 1
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Probing Slow Time Scale Dynamics at Methyl-Containing Side Chains in Proteins by Relaxation Dispersion NMR Measurements: Application to Methionine Residues in a Cavity Mutant of T4 Lysozyme. https://app.cochat.ai/papers/10.1021/ja004179p
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- Skrynnikov, N. R., Mulder, F. A. A., Hon, B., Dahlquist, F. W., & Kay, L. E. (2001). Probing Slow Time Scale Dynamics at Methyl-Containing Side Chains in Proteins by Relaxation Dispersion NMR Measurements: Application to Methionine Residues in a Cavity Mutant of T4 Lysozyme. Journal of the American Chemical Society. https://doi.org/10.1021/ja004179p
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
