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An Improved 15N Relaxation Dispersion Experiment for the Measurement of Millisecond Time-Scale Dynamics in Proteins
Abstract
A new (15)N constant-time relaxation dispersion pulse scheme for the quantification of millisecond time-scale exchange dynamics in proteins is presented. The experiment differs from previously developed sequences in that it includes (1)H continuous-wave decoupling during the (15)N Carr-Purcell-Meiboom-Gill (CPMG) pulse train that significantly improves the relaxation properties of (15)N magnetization, leading to sensitivity gains in experiments. Moreover, it is shown that inclusion of an additional (15)N 180 degrees refocusing pulse (phase cycled +/- x) in the center of the CPMG pulse train, consisting of 1(5)N 180 degrees (y) pulses, provides compensation for pulse imperfections beyond the normal CPMG scheme. Relative to existing relaxation-compensated constant-time relaxation dispersion pulse schemes, nu(CPMG) values that are only half as large can be employed, offering increased sensitivity to slow time-scale exchange processes. The robustness of the methodology is illustrated with applications involving a pair of proteins: an SH3 domain that does not show millisecond time-scale exchange and an FF domain with significant chemical exchange contributions.
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Cited by
Studying “Invisible” Excited Protein States in Slow Exchange with a Major State Conformation
Vallurupalli, P., Bouvignies, G., & Kay, L. E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3001419 · Cited by 526
Self-citationStructure of an Intermediate State in Protein Folding and Aggregation
Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 398
Self-citationA Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Korzhnev, D. M., Religa, T. L., Banachewicz, W., Fersht, A. R., & Kay, L. E. (2010) · Science · doi:10.1126/science.1191723 · Cited by 305
Self-citationChemical exchange in biomacromolecules: Past, present, and future
Palmer, A. G. (2014) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2014.01.008 · Cited by 263
Design of amyloidogenic peptide traps
Sahtoe, D. D., Andrzejewska, E. A., Han, H. L., Rennella, E., Schneider, M. M., Meisl, G., Ahlrichs, M., Decarreau, J., Nguyen, H., Kang, A., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01578-5 · Cited by 48
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Metadata
- Authors
- Hansen, D. F., Vallurupalli, P., & Kay, L. E.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-11-15
- Volume
- 112
- Issue
- 19
- Pages
- 5898-5904
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2047695660
- Cited by
- 232
- References
- 0
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hansen, D. F., Vallurupalli, P., & Kay, L. E. (2008). An Improved 15N Relaxation Dispersion Experiment for the Measurement of Millisecond Time-Scale Dynamics in Proteins. The Journal of Physical Chemistry B. https://doi.org/10.1021/jp074793o
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