Olga Torres, Barbara Procacci, Meghan E. Halse, Ralph W. Adams, Damir Blazina, Simon B. Duckett, Beatriz Eguillor, Richard A. Green, Robin N. Perutz and David C. Williamson
Journal of the American Chemical Society
DOI: 10.1021/ja504732u
[NMR paper] Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
J Biomol NMR. 2013 Oct 9;
...
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Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Yi Xue, Joshua M. Ward, Tairan Yuwen, Ivan S. Podkorytov and Nikolai R. Skrynnikov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206442c/aop/images/medium/ja-2011-06442c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206442c
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http://feeds.feedburner.com/~r/acs/jacsat/~4/NvRRKHU2H3k
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[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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11-19-2010 08:32 PM
[NMR paper] Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
Related Articles Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
J Biomol Struct Dyn. 1999 Aug;17(1):157-74
Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies...
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11-18-2010 08:31 PM
Probing Microsecond Time Scale Dynamics in Proteins by Methyl 1H Carr-Purcell-Meiboom
Probing Microsecond Time Scale Dynamics in Proteins by Methyl 1H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrCr
Renee Otten, Janice Villali, Dorothee Kern and Frans A. A. Mulder
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107410x/aop/images/medium/ja-2010-07410x_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107410x
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11-17-2010 06:08 PM
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meibo
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrC(r).
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrC(r).
J Am Chem Soc. 2010 Nov 8;
Authors: Otten R, Villali J, Kern D, Mulder FA
To study microsecond processes by relaxation dispersion NMR spectroscopy, low power...
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11-10-2010 02:29 PM
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Si
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
Related Articles Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
J Am Chem Soc. 2010 Aug 6;
Authors: Krushelnitsky A, Zinkevich T, Reichert D, Chevelkov V, Reif B
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic...
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08-17-2010 03:36 AM
Monitoring H-D exchange on second time scale with Frydman NMR spectroscopy
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Real-Time Monitoring of Chemical Transformations by Ultrafast 2D NMR Spectroscopy
Maayan Gal, Mor Mishkovsky, and Lucio Frydman
J. Am. Chem. Soc.; 2006; 128(3) pp 951 - 956;
Abstract:
Photochemical Pump and NMR Probe: Chemically Created NMR Coherence on a Microsecond Time Scale
Linear Mode
