Analysis of 15N–1H NMR Relaxation in Proteins by a Combined Experimental and Molecular Dynamics Simulation Approach: Picosecond–Nanosecond Dynamics of the Rho GTPase Binding Domain of Plexin-B1 in the Dimeric State Indicates Allosteric Pathways-Reference-Cited by-同舟云学术

Analysis of 15N–1H NMR Relaxation in Proteins by a Combined Experimental and Molecular Dynamics Simulation Approach: Picosecond–Nanosecond Dynamics of the Rho GTPase Binding Domain of Plexin-B1 in the Dimeric State Indicates Allosteric Pathways

Published:2012-12-28 Issue:1 Volume:117 Page:174-184
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Zerbetto Mirco¹,Anderson Ross²,Bouguet-Bonnet Sabine³,Rech Mariano¹,Zhang Liqun²,Meirovitch Eva⁴,Polimeno Antonino¹,Buck Matthias²

Affiliation:

1. Dipartimento di Scienze Chimiche, Università degli Studi di Padova, Padova 35131, Italy

2. Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106-7169, United States

3. Methodologie RMN, Faculté des Sciences et Techniques, Nancy-Université, Nancy 54500, France

4. The Mina & Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp310142f

Reference58 articles.

1. NMR Characterization of the Dynamics of Biomacromolecules

2. New Tools Provide New Insights in NMR Studies of Protein Dynamics

3. Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution

4. Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional Consequences

5. Variability of the 15N Chemical Shielding Tensors in the B3 Domain of Protein G from 15N Relaxation Measurements at Several Fields. Implications for Backbone Order Parameters

Cited by 27 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Local Structures in Proteins from Microsecond Molecular Dynamics Simulations: 2. The Role of Symmetry in GTPase Binding and Dimer Formation;The Journal of Physical Chemistry B;2024-02-13

2. Local Structures in Proteins from Microsecond Molecular Dynamics Simulations: A Symmetry-Based Perspective;The Journal of Physical Chemistry B;2024-02-13

3. Microsecond MD Simulations of the Plexin-B1 RBD: N–H Probability Density as Descriptor of Structural Dynamics, Dimerization-Related Conformational Entropy, and Transient Dimer Asymmetry;The Journal of Physical Chemistry B;2022-08-18

4. Microsecond MD Simulations of the Plexin-B1 RBD: 2. N–H Probability Densities and Conformational Entropy in Ligand-Free, Rac1-Bound, and Dimer RBD;The Journal of Physical Chemistry B;2022-08-17

5. Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy;Pharmacology & Therapeutics;2022-08