Rotational-Echo Double Resonance Characterization of Vancomycin Binding Sites inStaphylococcus aureus†

Biochemistry ◽  
2002 ◽  
Vol 41 (22) ◽  
pp. 6967-6977 ◽  
Author(s):  
Sung Joon Kim ◽  
Lynette Cegelski ◽  
Daniel R. Studelska ◽  
Robert D. O'Connor ◽  
Anil K. Mehta ◽  
...  
Keyword(s):  
Binding Sites ◽  
Double Resonance ◽  
Rotational Echo Double Resonance

Rotational-Echo Double Resonance Characterization of the Effects of Vancomycin on Cell Wall Synthesis inStaphylococcus aureus†

Biochemistry ◽  
2002 ◽  
Vol 41 (43) ◽  
pp. 13053-13058 ◽  
Author(s):  
Lynette Cegelski ◽  
Sung Joon Kim ◽  
Andrew W. Hing ◽  
Daniel R. Studelska ◽  
Robert D. O'Connor ◽  
...  
Keyword(s):  
Cell Wall ◽  
Double Resonance ◽  
Cell Wall Synthesis ◽  
Rotational Echo Double Resonance

Long-Range Distance Measurements of Protein Binding Sites by Rotational-Echo Double-Resonance NMR

1996 ◽  
Vol 118 (23) ◽  
pp. 5476-5477 ◽  
Author(s):  
Daniel R. Studelska ◽  
Christopher A. Klug ◽  
Denise D. Beusen ◽  
Lynda M. McDowell ◽  
Jacob Schaefer
Keyword(s):  
Protein Binding ◽  
Long Range ◽  
Binding Sites ◽  
Double Resonance ◽  
Distance Measurements ◽  
Protein Binding Sites ◽  
Rotational Echo Double Resonance

scholarly journals Characterization of Interfacial Structure in Polymer-Fullerene Bulk Heterojunctions via C13 {H2} Rotational Echo Double Resonance NMR

2018 ◽  
Vol 121 (2) ◽  
Author(s):  
R. C. Nieuwendaal ◽  
D. M. DeLongchamp ◽  
L. J. Richter ◽  
C. R. Snyder ◽  
R. L. Jones ◽  
...  
Keyword(s):  
Double Resonance ◽  
Interfacial Structure ◽  
Bulk Heterojunctions ◽  
Rotational Echo Double Resonance

Characterization of Thromboxane A2/Prostaglandin H2 Receptors in Porcine Coronary Artery -The Inhibitory Effect of a Novel Dibenzoxepin Derivative, KW-3635

1992 ◽  
Vol 67 (05) ◽  
pp. 582-584 ◽  
Author(s):  
Ichiro Miki ◽  
Akio Ishii
Keyword(s):  
Coronary Artery ◽  
Binding Sites ◽  
Thromboxane A2 ◽  
Inhibitory Effect ◽  
Scatchard Analysis ◽  
Single Class ◽  
Porcine Coronary Artery ◽  
Equilibrium Binding ◽  
H2 Receptors

SummaryWe characterized the thromboxane A2/prostaglandin H2 receptors in porcine coronary artery. The binding of [3H]SQ 29,548, a thromboxane A2 antagonist, to coronary arterial membranes was saturable and displaceable. Scatchard analysis of equilibrium binding showed a single class of high affinity binding sites with a dissociation constant of 18.5 ±1.0 nM and the maximum binding of 80.7 ± 5.2 fmol/mg protein. [3H]SQ 29,548 binding was concentration-dependently inhibited by thromboxane A2 antagonists such as SQ 29,548, BM13505 and BM13177 or the thromboxane A2 agonists such as U46619 and U44069. KW-3635, a novel dibenzoxepin derivative, concentration-dependently inhibited the [3H]SQ 29,548 binding to thromboxane A2/prosta-glandin H2 receptors in coronary artery with an inhibition constant of 6.0 ± 0.69 nM (mean ± S.E.M.).

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