scholarly journals High‐Resolution 31P Field Cycling NMR as a Probe of Substrates Dynamics on GMP Reductase

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Masha Rosenberg ◽  
Alfred Redfield ◽  
Mary Roberts ◽  
Lizbeth Hedstrom
Author(s):  
Mary F. Roberts ◽  
Jingfei Cai ◽  
Sivanandam V. Natarajan ◽  
Hanif M. Khan ◽  
Nathalie Reuter ◽  
...  

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Mary Fedarko Roberts ◽  
Mingming Pu ◽  
Alfred G. Redfield

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Mary Roberts ◽  
Boguslaw Stec ◽  
Cheryl Gradziel ◽  
Yang Wei ◽  
Alfred Redfield

2021 ◽  
Author(s):  
Mary Roberts ◽  
Jingfei Cai ◽  
V.N. Sivanandam ◽  
Hanif M. Khan ◽  
Nathalie Reuter ◽  
...  

High resolution field cycling <sup>31</sup>P NMR spin-lattice relaxometry, where the sample is excited at high field, shuttled in the magnet bore for low field relaxation, then shuttled back to high field for readout of the residual magnetization, provides data on phospholipid dynamics and structure. In the field range from 11.74 down to 0.003 T three dipolar nuclear magnetic relaxation dispersions (NMRDs) and one due to <sup>31</sup>P chemical shift anisotropy contribute to R<sub>1 </sub>of phospholipids<sub>.</sub> Extraction of correlation times and maximum relaxation amplitudes for these NMRDs provides (1) lateral diffusion constants for different phospholipids in the same bilayer (illustrated with phospholipase C binding), (2) estimates of how additives alter the motion of the phospholipid about its long axis (looking at cholesterol effects), and (3) an average <sup>31</sup>P – <sup>1</sup>H angle with respect to the bilayer normal, which reveals that polar head group motion is not restricted on a µs timescale. Although this deals exclusively with phospholipids in small unilamellar vesicles, these same NMRDs can be measured for phospholipids in micelles and nanodiscs, making this technique useful for monitoring lipid behavior in a variety of structures.


Biochemistry ◽  
2004 ◽  
Vol 43 (12) ◽  
pp. 3637-3650 ◽  
Author(s):  
Mary F. Roberts ◽  
Qizhi Cui ◽  
Christopher J. Turner ◽  
David A. Case ◽  
Alfred G. Redfield

Biochemistry ◽  
2020 ◽  
Vol 59 (25) ◽  
pp. 2359-2370
Author(s):  
Masha M. Rosenberg ◽  
Tianjiong Yao ◽  
Gregory C. Patton ◽  
Alfred G. Redfield ◽  
Mary F. Roberts ◽  
...  

2009 ◽  
Vol 97 (1) ◽  
pp. 132-141 ◽  
Author(s):  
Mary F. Roberts ◽  
Alfred G. Redfield ◽  
Udayan Mohanty

2009 ◽  
Vol 37 (1-4) ◽  
pp. 515-537 ◽  
Author(s):  
S. E. Korchak ◽  
A. S. Kiryutin ◽  
K. L. Ivanov ◽  
A. V. Yurkovskaya ◽  
Yu. A. Grishin ◽  
...  

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