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
 

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
 

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
 

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:10.007/s10858-015-9919-6>
PMID: 25828256      PMCID: PMC4819240
 

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
 

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]
 

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
 

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
 

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
 

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
 

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
 

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     
 

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
 

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>
 

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>
 

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     
 

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     
 

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