Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes
Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes
Alexandar L. Hansen, Patrik Lundstrom, Algirdas Velyvis and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210711v/aop/images/medium/ja-2011-10711v_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210711v
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Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Abstract A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly 13C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold via a partially structured low populated intermediate that interconverts with the folded, ground state on the millisecond time-scale....
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06-20-2011 03:31 PM
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
J Biomol NMR. 2011 Jun 18;
Authors: Hansen AL, Kay LE
A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has...
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06-18-2011 01:10 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
13CHD2 Methyl Group Probes of Millisecond Time Scale Exchange in Proteins by 1H Relax
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/2010/jacsat.2010.132.issue-32/ja104578n/production/images/medium/ja-2010-04578n_0005.gif
<!-- abstract content --><sup>13</sup>CHD<sub>2</sub> Methyl Group Probes of Millisecond Time Scale Exchange in Proteins by <sup>1</sup>H Relaxation Dispersion: An Application to Proteasome Gating Residue Dynamics
Andrew J. Baldwin, Tomasz L. Religa, D. Flemming Hansen, Guillaume Bouvignies and Lewis E. Kay*
Departments of Molecular Genetics, Biochemistry and Chemistry,...
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
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