Protein dynamics in the solid-state from 2H NMR lineshape analysis. III. MOMD in the presence of Magic Angle Spinning
E. Meirovitch, Z. Liang, J. H. Freed.
Solid State Nucl. Magn. Reson. 89, 35-44 (2018)
<doi:10.1016/j.ssnmr.2017.11.001>
PMID: 29208317
PMCID: PMC5772661
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Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: the Role of Site Symmetry
O. Tchaicheeyan, J. H. Freed, and E. Meirovitch.
J. Phys. Chem. B 120 2886-2898 (2016)
Supporting Information
<doi:10.1021/acs.jpcb.6b00524>
PMID: 26938937
PMCID: PMC4837759
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Protein Dynamics in the Solid State from 2H NMR Line Shape Analysis. II. MOMD Applied to C–D and C–CD3 Probes
E. Meirovitch, Z. Liang, and J. H. Freed.
J. Phys. Chem. B 119 14022-14032 (2015)
<doi:10.1021/acs.jpcb.5b07434>
PMID: 26402431
PMCID: PMC4676681
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Dynamic Nuclear Polarization of Membrane Proteins: Covalently Bound Spin-Labels at Protein-Protein Interfaces
B.J. Wylie, B.G. Dzikovski, S. Pawsey, M. Caporini, M. Rosay, J.H. Freed, A.E. McDermott.
J. Biomol. NMR 61, 361-367 (2015).
<doi:10.1007/s10858-015-9919-6>
PMID: 25828256
PMCID: PMC4819240
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Protein Dynamics in the Solid State from 2H NMR Line Shape Analysis: A Consistent Perspective
E. Meirovitch, Z. Liang, and J.H. Freed.
J. Phys. Chem B 119, 2857-2868 (2015).
<doi:10.1021/jp511386b>
PMID: 25594631
PMCID: PMC4358757
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Protein Dynamics by NMR Spin Relaxation: The Slowly Relaxing Local Structure Perspective
E. Meirovitch, A. Polimeno, and J.H. Freed.
In E. Mag. Res. Online, R.K. Harris and R.L. Wasylishen, Eds.
John Wiley & Sons, Inc.: New York, 2011; pp 1-9.
<doi:10.1002/9780470034590.emrstm1243>
PMID: [None - Book]
PMCID: [None - Book]
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Methyl Dynamics of a Ca2+-Calmodulin-Peptide Complex from NMR/SRLS
Y.E. Shapiro, A. Polimeno, J.H. Freed, and E. Meirovitch.
J. Phys. Chem. B 115, 354-365 (2011).
<doi:10.1021/jp107130m>
PMID: 21166433
PMCID: PMC3062514
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Backbone Dynamics of Deoxy and Carbonmonoxy Hemoglobin by NMR/SRLS
E. Meirovitch, M. Zerbetto, A. Polimeno, and J.H. Freed.
J. Phys. Chem. B 115, 143-157 (2011).
<doi:10.1021/jp107553j>
PMID: 21162544
PMCID: PMC3071157
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Comment on "The physical basis of model-free analysis of NMR relaxation data from proteins and complex fluids" [J. Chem. Phys. 131, 224507 (2009)]
E. Meirovitch, A. Polimeno, and J.H. Freed.
J. Chem. Phys. 132, 207101 (2010).
<doi:10.1063/1.3429599>
PMID: 20515116
PMCID: PMC2887917
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Structural Dynamics of Bio-Macromolecules by NMR: The Slowly Relaxing Local Structure Approach
E. Meirovitch, Y.E. Shapiro, A. Polimeno, J.H. Freed.
Progress in NMR Spectroscopy, 56, 360-405 (2010).
<doi:10.1016/j.pnmrs.2010.03.002>
PMID: 20625480
PMCID: PMC2899824
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An Improved Picture of Methyl Dynamics in Proteins from Slowly Relaxing Local Structure Analysis of 2H Spin Relaxation
E. Meirovitch, Y.E. Shapiro, A. Polimeno, and J.H. Freed.
J. Phys. Chem. B 111, 12865-12875 (2007).
<doi:10.1021/jp072156s>
PMID: 17941658
PMCID: PMC2885794
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Methyl Dynamics in Proteins from NMR Slowly Relaxing Local Structure Spin Relaxation Analysis: A New Perspective
Eva Meirovitch, Antonino Polimeno, and Jack H. Freed.
J. Phys. Chem. B 110, 20615-20628 (2006).
<doi:10.1021/jp061403+>
PMID: 17034251
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Protein Dynamics from NMR: The Slowly Relaxing Local Structure Analysis Compared with Model-Free Analysis
E. Meirovitch, Y.E. Shapiro, A. Polimeno, and J.H. Freed.
J. Phys. Chem. A 110, 8366-8396 (2006).
<doi:10.1021/jp056975t>
PMID: 16821820
PMCID: PMC2758167
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Mode-Coupling SRLS versus Mode-Decoupled Model-Free N-H Bond Dynamics: Mode-Mixing and Renormalization
E. Meirovitch, Y.E. Shapiro, Z. Liang, and J.H. Freed.
J. Phys. Chem. B 107, 9898-9904 (2003).
<doi:10.1021/jp030502>
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Mode-Coupling Analysis of 15N CSA-15N-1H Dipolar Cross-Correlation in Proteins. Rhombic Potentials at the N-H Bond
E. Meirovitch, Y.E. Shapiro, V. Tugarinov, Z. Liang, and J.H. Freed.
J. Phys. Chem. B 107, 9883-9897 (2003).
<doi:10.1021/jp030501h>
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Domain Flexibility in Ligand-Free and Inhibitor-Bound Escherichia coli Adenylate Kinase Based on a Mode-Coupling Analysis of 15N Spin Relaxation
Y.E. Shapiro, E. Kahana, V. Tugarinov, Z. Liang, J.H. Freed, and E. Meirovitch.
Biochemistry 41, 6271-6281 (2002).
Supporting Information
<doi:10.1021/bi012132q>
PMID: 12009888
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A Novel View of Domain Flexibility in E. coli Adenylate Kinase Based on Structural Mode-Coupling 15N NMR Relaxation
V. Tugarinov, Y.E. Shapiro, Z. Liang, J.H. Freed and E. Meirovitch.
J. Mol. Biol. 315, 155-170 (2002).
Supporting Information
<doi:10.1006/jmbi.2001.5231>
PMID: 11779236
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A Structural Mode-Coupling Approach to 15N NMR Relaxation in Proteins
V. Tugarinov, Z. Liang, Y.E. Shapiro, J.H. Freed, and E. Meirovitch.
J. Am. Chem. Soc. 123, 3055-3063 (2001).
Supporting Information
<doi:10.1021/ja003803v>
PMID: 11457016
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