Determination of the Rotational Diffusion Tensor of Macromolecules in Solution from NMR Relaxation Data with a Combination of Exact and Approximate Methods—Application to the Determination of Interdomain Orientation in Multidomain Proteins

2001 ◽  
Vol 149 (2) ◽  
pp. 204-217 ◽  
Author(s):  
Ranajeet Ghose ◽  
David Fushman ◽  
David Cowburn
Keyword(s):  
Diffusion Tensor ◽  
Rotational Diffusion ◽  
Nmr Relaxation ◽  
Multidomain Proteins ◽  
Relaxation Data ◽  
Approximate Methods ◽  
Rotational Diffusion Tensor ◽  
Exact And Approximate Methods

Molecular motion and methyl group rotation barriers from 13C nmr relaxation times. Podacarpic acid derivatives

1982 ◽  
Vol 60 (10) ◽  
pp. 1173-1177 ◽  
Author(s):  
Helmut Beierbeck ◽  
John W. Easton ◽  
John K. Saunders ◽  
Russell A. Bell
Keyword(s):  
Diffusion Tensor ◽  
Rotational Diffusion ◽  
Relaxation Times ◽  
Nmr Relaxation ◽  
Time Data ◽  
Nmr Relaxation Times ◽  
Group Rotation ◽  
Rotational Diffusion Tensor ◽  
Nmr Relaxation Time ◽  
C Nmr

The 13C nmr relaxation time data for a number of compounds related to podocarpic acid are presented. The T1 values of these molecules were satisfactorily reproduced by application of Woessner's equations for an asymmetric top assuming that the preferred principal axis of the rotational diffusion tensor was either the preferred principal inertial axis or an axis containing the centre of mass and the heterosubstituent at C-4. The values for hindrance to rotation for the various methyl groups are given and their variations discussed.

Determination of the molecular rotational-diffusion tensor for liquid ethyl bromide

1982 ◽  
Vol 17 (5) ◽  
pp. 458-464
Author(s):  
V. A. Daragan ◽  
I. V. Zlokazova ◽  
N. K. Gaisin ◽  
Kh. Z. Khusainov
Keyword(s):  
Diffusion Tensor ◽  
Rotational Diffusion ◽  
Ethyl Bromide ◽  
Rotational Diffusion Tensor

scholarly journals How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?

2021 ◽  
Vol 75 (2-3) ◽  
pp. 119-131
Author(s):  
Albert A. Smith ◽  
Nicolas Bolik-Coulon ◽  
Matthias Ernst ◽  
Beat H. Meier ◽  
Fabien Ferrage
Keyword(s):  
Nuclear Magnetic Resonance ◽  
High Resolution ◽  
High Field ◽  
Rotational Diffusion ◽  
Relaxation Data ◽  
Internal Dynamics ◽  
Nmr Relaxometry ◽  
Analysis Of Dynamics

AbstractThe dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments—where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolution—seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the “detector” analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-13 relaxometry in the small protein ubiquitin. We show that relaxometry data leads to better information about nanosecond motions as compared to high-field relaxation data only. Our calculations show that gains from relaxometry are greater with increasing correlation time of rotational diffusion.

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