NMR spectroscopy to study the dynamics and interactions of CFTR.
Methods Mol Biol. 2011;741:377-403
Authors: Kanelis V, Chong PA, Forman-Kay JD
Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) is a multi-domain membrane chloride channel whose activity is regulated by ATP at two nucleotide-binding domains (NBD1 and NBD2) and by phosphorylation of the regulatory (R) region. The NBDs and the R region have functionally relevant motions that are critical for channel gating. Nuclear magnetic resonance (NMR) spectroscopy is a highly useful technique for obtaining information on the structure and interactions of CFTR and is extremely powerful for probing dynamics. NMR approaches for studying CFTR are reviewed, using our previous NBD1 and the R region results to provide examples. These NMR data are yielding insights into the dynamic properties and interactions that facilitate normal CFTR regulation as well as pathological effects of mutations, including the most common disease mutant, deletion of F508 in NBD1.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
Chembiochem. 2011 Mar 21;12(5):695-9
Authors: Potenza D, Vasile F, Belvisi L, Civera M, Araldi EM
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13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
Ce?dric Laguri, Nicolas Sapay, Jean-Pierre Simorre, Bernhard Brutscher, Anne Imberty, Pierre Gans and Hugues Lortat-Jacob
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201753e/aop/images/medium/ja-2011-01753e_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201753e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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05-04-2011 04:14 PM
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Methods Enzymol. 2010;478:305-22
Authors: Yamaguchi Y, Kato K
Unique advantages offered by nuclear magnetic resonance (NMR) spectroscopy provide high-resolution information not only on structures but also on dynamics and interactions of glycoconjugates in solution. These benefits are further enhanced by applying stable-isotope-labeling techniques, which we...
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[NMR paper] An NMR spectroscopy study of bendaline-albumin interactions.
An NMR spectroscopy study of bendaline-albumin interactions.
Related Articles An NMR spectroscopy study of bendaline-albumin interactions.
Bioorg Chem. 2003 Oct;31(5):378-88
Authors: Delfini M, Bianchetti C, Di Cocco ME, Pescosolido N, Porcelli F, Rosa R, Rugo G
The complete assignment of the 1H and 13C NMR spectra of bendaline (BNDL) was performed by mono-dimensional and homo- and hetero-correlated two-dimensional NMR experiments. The interaction between bendaline and albumin was also studied by the analysis of the motional parameters...
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11-24-2010 09:16 PM
[NMR paper] DNA-XPA interactions: a (31)P NMR and molecular modeling study of dCCAATAACC associat
DNA-XPA interactions: a (31)P NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA.
Related Articles DNA-XPA interactions: a (31)P NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA.
Nucleic Acids Res. 2001 Jun 15;29(12):2635-43
Authors: Buchko GW, Tung CS, McAteer K, Isern NG, Spicer LD, Kennedy MA
Recent NMR-based, chemical shift mapping...
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11-19-2010 08:32 PM
[NMR paper] Dynamics of stromelysin/inhibitor interactions studied by 15N NMR relaxation measurem
Dynamics of stromelysin/inhibitor interactions studied by 15N NMR relaxation measurements: comparison of ligand binding to the S1-S3 and S'1-S'3 subsites.
Related Articles Dynamics of stromelysin/inhibitor interactions studied by 15N NMR relaxation measurements: comparison of ligand binding to the S1-S3 and S'1-S'3 subsites.
J Biomol NMR. 1999 Sep;15(1):55-64
Authors: Yuan P, Marshall VP, Petzold GL, Poorman RA, Stockman BJ
This report describes the backbone amide dynamics of the uniformly 15N labeled catalytic domain of human stromelysin...
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[NMR paper] NMR study of collagen-water interactions.
NMR study of collagen-water interactions.
Related Articles NMR study of collagen-water interactions.
Biopolymers. 1994 Dec;34(12):1615-26
Authors: Renou JP, Bonnet M, Bielicki G, Rochdi A, Gatellier P
A proton magnetic resonance study of different cross-linked collagens was performed as a function of water content and temperature. Collagens from three connective tissues (calf, steer, and cow) were chosen according to the different number of nonreducible multivalent cross-links, which increases during the life of animal. Samples were hydrated...
NMR spectroscopy to study the dynamics and interactions of CFTR.
Linear Mode
