DOI: 10.1110/ps.041139505. Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR <i>R</i><sub>1ρ</sub> relaxation experiments

Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments

10.1110/ps.041139505

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractNMR spin relaxation experiments are used to characterize the dynamics of the backbone of ubiquitin. Chemical exchange processes affecting residues Ile 23, Asn 25, Thr 55, and Val 70 are characterized using on‐ and off‐resonance rotating‐frame 15N R1ρ relaxation experiments to have a kinetic exchange rate constant of 25,000 sec−1 at 280 K. The exchange process affecting residues 23, 25, and 55 appears to result from disruption of N‐cap hydrogen bonds of the α‐helix and possibly from repacking of the side chain of Ile 23. Chemical exchange processes affecting other residues on the surface of ubiquitin are identified using 1H‐15N multiple quantum relaxation experiments. These residues are located near or at the regions known to interact with various enzymes of the ubiquitin‐dependent protein degradation pathway.

Bibliography

Massi, F., Grey, M. J., & Palmer, A. G. (2005). Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1Ï relaxation experiments. Protein Science, 14(3), 735â742. Portico.

Authors 3

Francesca Massi (first)
Michael J. Grey (additional)
Arthur G. Palmer (additional)

References 50 Referenced 128

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Dates

Type	When
Created	20 years, 6 months ago (Feb. 18, 2005, 2:52 p.m.)
Deposited	1 year, 10 months ago (Oct. 12, 2023, 6:41 p.m.)
Indexed	3 weeks, 1 day ago (Aug. 2, 2025, 12:24 a.m.)
Issued	20 years, 5 months ago (March 1, 2005)
Published	20 years, 5 months ago (March 1, 2005)
Published Online	16 years, 7 months ago (Jan. 1, 2009)
Published Print	20 years, 5 months ago (March 1, 2005)

Funders 0

None

BibTeX

@article{Massi_2005, title={Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments}, volume={14}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.041139505}, DOI={10.1110/ps.041139505}, number={3}, journal={Protein Science}, publisher={Wiley}, author={Massi, Francesca and Grey, Michael J. and Palmer, Arthur G.}, year={2005}, month=mar, pages={735–742} }

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