Related ArticlesOn the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
J Biochem. 1991 Jan;109(1):144-9
Authors: Fujii S, Nonaka Y, Okamoto M, Miura R
The interaction between 2',5'-ADP and NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria was examined by titrating the enzyme with 2',5'-ADP, while the 31P-signals of 2',5'-ADP were being monitored by 31P-NMR. From the titration profile, the dissociation constant for the complex of the enzyme with 2',5'-ADP was estimated to be 0.22 +/- 0.05 mM. Adrenodoxin reductase was reconstituted with 13C-enriched FADs. The 13C-enriched FADs used were [2-13C]-, [4,10 alpha-13C2]-, and [4 alpha-13C]FAD. The 13C-NMR spectra of these reconstituted enzyme preparations showed 13C-resonance peaks corresponding to the enriched carbon atoms at 160.6 , 165.1, 136.6, and 152.4 ppm (2-, 4-, 4 alpha-, and 10 alpha-13C atoms, respectively). When 2',5'-ADP was bound to the reconstituted enzyme, these 13C-resonance peaks did not shift appreciably from those of the unbound enzyme, whereas in the complex of the reconstituted enzyme with NADP+, the signals for 4- and 10 alpha-13C shifted to higher fields by 2.1 and 0.7 ppm, respectively and the 4 alpha-13C signal shifted to a lower field by 1.4 ppm. These results suggest that in the complex of the enzyme with NADP+ the pyridine moiety is located in the vicinity of C(4 alpha)-C(4) region and that the pi-electron density of the 4 alpha-position of flavin is decreased in the enzyme-NADP+ complex. This argues in favor of the electron transfer from the dihydropyridine moiety of NADPH to the electron-deficient N(5) = C(4 alpha) region of flavin.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
J Mol Graph Model. 2011 Sep 3;
Authors: Fukunishi Y, Mizukoshi Y, Takeuchi K, Shimada I, Takahashi H, Nakamura H
Abstract
We developed a new protein-ligand docking calculation method using experimental NMR data. Recently, we proposed a novel ligand epitope-mapping experiment, which utilizes the difference between the longitudinal relaxation rates of ligand protons with and...
[Question from NMRWiki Q&A forum] protein-ligand interactions 2D NMR
protein-ligand interactions 2D NMR
I want to judge ligand protein interactions. Mine one is a dimer protein. Other than HSQC perturbation which other 2DNMR experiments useful to know the interaction?
Check if somebody has answered this question on NMRWiki QA forum
[NMR paper] NMR studies of protein-ligand interactions.
NMR studies of protein-ligand interactions.
Related Articles NMR studies of protein-ligand interactions.
Methods Mol Biol. 2005;305:197-214
Authors: Maurer T
Interaction between biological macromolecules or of macromolecules with low-molecular-weight ligands is a central paradigm in the understanding of function in biological systems. It is also the major goal in pharmaceutical research to find and optimize ligands that modulate the function of biological macromolecules. Both technological advances and new methods in the field of nuclear...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] Studies of protein-ligand interactions by NMR.
Studies of protein-ligand interactions by NMR.
Related Articles Studies of protein-ligand interactions by NMR.
Methods Mol Biol. 1997;60:195-232
Authors: Craik DJ, Wilce JA
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Studies of protein-ligand interactions by NMR.
Studies of protein-ligand interactions by NMR.
Related Articles Studies of protein-ligand interactions by NMR.
Methods Mol Biol. 1997;60:195-232
Authors: Craik DJ, Wilce JA
nmrlearner
Journal club
0
08-22-2010 03:03 PM
A solution model of the complex formed by adrenodoxin and adrenodoxin reductase deter
A solution model of the complex formed by adrenodoxin and adrenodoxin reductase determined by paramagnetic NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A solution model of the complex formed by adrenodoxin and adrenodoxin reductase determined by paramagnetic NMR spectroscopy.
Biochemistry. 2010 Aug 17;49(32):6846-55
Authors: Keizers PH, Mersinli B, Reinle W, Donauer J, Hiruma Y, Hannemann F, Overhand M, Bernhardt R, Ubbink M
Lanthanide tags offer the opportunity to...
On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase a
Linear Mode
