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Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme
Abstract
A new CPMG-based multiple quantum relaxation dispersion experiment is presented for measuring millisecond dynamic processes at side-chain methyl positions in high molecular weight proteins. The experiment benefits from a methyl-TROSY effect in which cancellation of intramethyl dipole fields occurs, leading to methyl (13)C-(1)H correlation spectra of high sensitivity and resolution (Tugarinov, V.; Hwang, P. M.; Ollerenshaw, J. E.; Kay, L. E. J. Am. Chem. Soc. 2003, 125, 10420-10428). The utility of the methodology is illustrated with an application to a highly deuterated, methyl-protonated sample of malate synthase G, an 82 kDa enzyme consisting of a single polypeptide chain. A comparison of the sensitivity obtained using the present approach relative to existing HSQC-type (13)C single quantum dispersion experiments shows a gain of a factor of 5.4 on average, significantly increasing the range of applications for this methodology.
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Citations
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Korzhnev, D. M., & Kay, L. E. (2008) · Accounts of Chemical Research · doi:10.1021/ar700189y · Cited by 268
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A distal regulatory region of a class I human histone deacetylase
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Metadata
- Authors
- Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., & Kay, L. E.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-03-01
- Volume
- 126
- Issue
- 12
- Pages
- 3964-3973
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1984830795
- Cited by
- 237
- References
- 0
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., & Kay, L. E. (2004). Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme. Journal of the American Chemical Society. https://doi.org/10.1021/ja039587i
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