Related Articles19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenase.
Biochem Biophys Res Commun. 1993 Sep 15;195(2):594-9
Authors: Hamman S, Atta M, Ehrenberg A, Wilkins P, Dalton H, Béguin C, Fontecave M
The relaxation rates of fluoride, determined by 19F NMR spectroscopy, were greatly increased in the presence of protein Mn-A, the manganese form of the hydroxylase component of methane monooxygenase. This demonstrates that F- interacts with the manganese center of protein Mn-A. On the contrary, protein Mn-R2, the manganese form of the small subunit of ribonucleotide reductase, had no effect on the relaxation rate of F-. This reflects differences between the two proteins in terms of the accessibility of the metal ion sites, despite the strong similarities of these sites.
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with T
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides.
(13)C/(15)N-(19)F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides.
J Am Chem Soc. 2010 Nov 24;
Authors: Huang W, Varani G, Drobny GP
The complex of the HIV TAR RNA with the viral regulatory protein Tat is of considerable interest, but the plasticity of this interaction has made it impossible so far to establish the structure of that complex. In order to explore a new approach to obtain structural information on...
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13C/15N-19F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Pep
13C/15N-19F Intermolecular REDOR NMR Study of the Interaction of TAR RNA with Tat Peptides
Wei Huang, Gabriele Varani and Gary P. Drobny
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1051439/aop/images/medium/ja-2010-051439_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1051439
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/bKQhcXWaqW0
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11-25-2010 07:22 AM
[NMR paper] High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritell
High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Related Articles High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Cell Mol Biol (Noisy-le-grand). 2004 Jun;50(4):311-6
Authors: Hata K, Kono R, Fujisawa M, Kitahara R, Kamatari YO, Akasaka K, Xu Y
We have investigated the effect of pressure and temperature on the structural and thermodynamic stability of a protein dihydrofolate reductase from a deep-sea bacterium Moritella profunda in its folate-bound...
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11-24-2010 09:51 PM
[NMR thesis] NMR study of fluoride ion diffusion in potassium-doped ?-PbF_2
NMR study of fluoride ion diffusion in potassium-doped ?-PbF_2
Cannon, David M. (1978) NMR study of fluoride ion diffusion in potassium-doped ?-PbF_2. Master's thesis, California Institute of Technology. http://resolver.caltech.edu/CaltechTHESIS:03292010-111321744
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08-27-2010 01:45 AM
[NMR paper] Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Solid State Nucl Magn Reson. 1996 Dec;7(3):193-201
Authors: Yang QX, Huang FY, Lin TH, Gelbaum L, Howell EE, Huang TH
We have employed deuterium NMR techniques to determine the dynamics of trimethoprim (TMP) in a binary complex with dihydrofolate reductase...
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08-22-2010 02:20 PM
[NMR paper] 1H and 31P NMR study of speciation in systems containing ADP, Al3+, and fluoride.
1H and 31P NMR study of speciation in systems containing ADP, Al3+, and fluoride.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H and 31P NMR study of speciation in systems containing ADP, Al3+, and fluoride.
J Inorg Biochem. 1995 Apr;58(1):29-47
Authors: Wang X, Simpson JH, Nelson DJ
It has been proposed that AlF4- can serve as a tetrahedral pseudophosphate bound to guanosine diphosphate (GDP) in G-protein systems. In a previous paper , 19F and 1H NMR were used to...
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08-22-2010 03:41 AM
[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Related Articles 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
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08-22-2010 03:33 AM
[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Related Articles 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and me
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