scholarly journals Critical dynamics at incommensurate phase transitions and NMR relaxation experiments

1999 ◽  
Vol 59 (17) ◽  
pp. 11226-11243 ◽  
Author(s):  
B. A. Kaufmann ◽  
F. Schwabl ◽  
U. C. Täuber
Keyword(s):  
Phase Transitions ◽  
Nmr Relaxation ◽  
Incommensurate Phase ◽  
Critical Dynamics ◽  
Relaxation Experiments

Conformational dynamics and thermodynamics of protein–ligand binding studied by NMR relaxation

2012 ◽  
Vol 40 (2) ◽  
pp. 419-423 ◽  
Author(s):  
Mikael Akke
Keyword(s):  
Ligand Binding ◽  
Bound States ◽  
Conformational Dynamics ◽  
Nmr Relaxation ◽  
Titration Calorimetry ◽  
Conformational Entropy ◽  
Chain Order ◽  
Ligand Interactions ◽  
Galectin 3 ◽  
Relaxation Experiments

Protein conformational dynamics can be critical for ligand binding in two ways that relate to kinetics and thermodynamics respectively. First, conformational transitions between different substates can control access to the binding site (kinetics). Secondly, differences between free and ligand-bound states in their conformational fluctuations contribute to the entropy of ligand binding (thermodynamics). In the present paper, I focus on the second topic, summarizing our recent results on the role of conformational entropy in ligand binding to Gal3C (the carbohydrate-recognition domain of galectin-3). NMR relaxation experiments provide a unique probe of conformational entropy by characterizing bond-vector fluctuations at atomic resolution. By monitoring differences between the free and ligand-bound states in their backbone and side chain order parameters, we have estimated the contributions from conformational entropy to the free energy of binding. Overall, the conformational entropy of Gal3C increases upon ligand binding, thereby contributing favourably to the binding affinity. Comparisons with the results from isothermal titration calorimetry indicate that the conformational entropy is comparable in magnitude to the enthalpy of binding. Furthermore, there are significant differences in the dynamic response to binding of different ligands, despite the fact that the protein structure is virtually identical in the different protein–ligand complexes. Thus both affinity and specificity of ligand binding to Gal3C appear to depend in part on subtle differences in the conformational fluctuations that reflect the complex interplay between structure, dynamics and ligand interactions.

Backbone dynamics of the CDK inhibitor p19INK4d studied by 15N NMR relaxation experiments at two field strengths

1998 ◽  
Vol 283 (1) ◽  
pp. 221-229 ◽  
Author(s):  
Christian Renner ◽  
Roland Baumgartner ◽  
Angelika A Noegel ◽  
Tad A Holak
Keyword(s):  
Nmr Relaxation ◽  
Backbone Dynamics ◽  
15N Nmr ◽  
Cdk Inhibitor ◽  
15N Nmr Relaxation ◽  
Relaxation Experiments ◽  
Field Strengths

Lattice Vibrations and Incommensurate Phase Transitions in K2SeO4, Rb2ZnCl4and K2ZnCl4

1985 ◽  
Vol 24 (S2) ◽  
pp. 778 ◽  
Author(s):  
P. Echegut ◽  
G. Hauret ◽  
F. Gervais ◽  
N. E. Massa
Keyword(s):  
Phase Transitions ◽  
Incommensurate Phase ◽  
Lattice Vibrations

Quantifying Lipari–Szabo modelfree parameters from 13CO NMR relaxation experiments

2006 ◽  
Vol 36 (2) ◽  
pp. 79-102 ◽  
Author(s):  
Tianzhi Wang ◽  
Daniel S. Weaver ◽  
Sheng Cai ◽  
Erik R. P. Zuiderweg
Keyword(s):  
Nmr Relaxation ◽  
Relaxation Experiments
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