A Digital rf Pulse Burst Generator for NMR Relaxation Experiments

1970 ◽  
Vol 41 (12) ◽  
pp. 1766-1770 ◽  
Author(s):  
V. Radeka ◽  
R. L. Chase ◽  
M. Petrinovic ◽  
J. A. Glasel
Keyword(s):  
Nmr Relaxation ◽  
Pulse Burst ◽  
Digital Rf ◽  
Relaxation Experiments ◽  
Rf Pulse

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

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

Triple resonance 15N NMR relaxation experiments for studies of intrinsically disordered proteins

2017 ◽  
Vol 69 (3) ◽  
pp. 133-146 ◽  
Author(s):  
Pavel Srb ◽  
Jiří Nováček ◽  
Pavel Kadeřávek ◽  
Alžbeta Rabatinová ◽  
Libor Krásný ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Nmr Relaxation ◽  
Disordered Proteins ◽  
15N Nmr ◽  
Triple Resonance ◽  
Intrinsically Disordered ◽  
15N Nmr Relaxation ◽  
Relaxation Experiments

scholarly journals How much entropy is contained in NMR relaxation parameters?

2021 ◽  
Author(s):  
Falk Hoffmann ◽  
Frans A. A. Mulder ◽  
Lars V. Schäfer
Keyword(s):  
Time Scales ◽  
Nmr Relaxation ◽  
Md Simulations ◽  
Side Chain ◽  
Thermodynamic Quantities ◽  
T4 Lysozyme ◽  
Time Dynamics ◽  
Relaxation Parameters ◽  
Relaxation Experiments ◽  
Short Time

Solution-state NMR relaxation experiments are the cornerstone to study internalprotein dynamics at atomic resolution on time scales that are faster than the overallrotational tumbling time,τR. Since the motions described by NMR relaxation pa-rameters are connected to thermodynamic quantities like conformational entropies, thequestion arises how much of the total entropy is contained within this tumbling time.Using all-atom molecular dynamics (MD) simulations of T4 lysozyme, we found thatentropy build-up is rather fast for the backbone, such that the majority of the entropyis indeed contained in the short-time dynamics. In contrast, the contribution of slowdynamics of side chains on time scales beyondτRon the side chain conformationalentropy is significant and should be taken into account for the extraction of accuratethermodynamic properties.

Proton NMR-Relaxation Dispersion in Meconium Solutions and Healthy Amniotic Fluid: Possible Applications to Medical Diagnosis

1982 ◽  
Vol 37 (5-6) ◽  
pp. 394-398 ◽  
Author(s):  
Georges J. Béné ◽  
Bernard Borcard ◽  
Volker Graf ◽  
Emile Hiltbrand ◽  
Patric Magnin ◽  
...  
Keyword(s):  
Relaxation Time ◽  
Amniotic Fluid ◽  
Medical Diagnosis ◽  
High Field ◽  
Relaxation Times ◽  
Nmr Relaxation ◽  
Field Measurements ◽  
Relaxation Dispersion ◽  
Longitudinal Relaxation Time ◽  
Relaxation Experiments

Abstract In order to show that for a possible application in medical diagnosis NMR-relaxation experiments at low Larmor frequencies (v0 ≤ 20 kHz) are more sensitive than the up to now done high field measurements in the MHz-range, we present dispersion curves (v0 = 50 Hz to 50 MHz) of the proton longitudinal relaxation time T1 and values of the transversal relaxation time T2 for the example of amniotic fluids. Only for Larmor frequencies below ≃ 100 kHz the relaxation times for healthy amniotic fluid and pathological meconium solutions are significantly different, whereas at high Larmor frequencies, i. e. in the conventional MHz-range, the observed changes are rather small.

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