Related ArticlesNovel NMR tools to study structure and dynamics of biomembranes.
Chem Phys Lipids. 2002 Jun;116(1-2):135-51
Authors: Gawrisch K, Eldho NV, Polozov IV
Nuclear magnetic resonance (NMR) studies on biomembranes have benefited greatly from introduction of magic angle spinning (MAS) NMR techniques. Improvements in MAS probe technology, combined with the higher magnetic field strength of modern instruments, enables almost liquid-like resolution of lipid resonances. The cross-relaxation rates measured by nuclear Overhauser enhancement spectroscopy (NOESY) provide new insights into conformation and dynamics of lipids with atomic-scale resolution. The data reflect the tremendous motional disorder in the lipid matrix. Transfer of magnetization by spin diffusion along the proton network of lipids is of secondary relevance, even at a long NOESY mixing time of 300 ms. MAS experiments with re-coupling of anisotropic interactions, like the 13C-(1)H dipolar couplings, benefit from the excellent resolution of 13C shifts that enables assignment of the couplings to specific carbon atoms. The traditional 2H NMR experiments on deuterated lipids have higher sensitivity when conducted on oriented samples at higher magnetic field strength. A very large number of NMR parameters from lipid bilayers is now accessible, providing information about conformation and dynamics for every lipid segment. The NMR methods have the sensitivity and resolution to study lipid-protein interaction, lateral lipid organization, and the location of solvents and drugs in the lipid matrix.
NMR spectroscopy to study the dynamics and interactions of CFTR.
NMR spectroscopy to study the dynamics and interactions of CFTR.
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...
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[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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11-24-2010 11:14 PM
[NMR paper] Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Related Articles Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
J Am Chem Soc. 2004 Dec 1;126(47):15320-1
Authors: Lemaître V, de Planque MR, Howes AP, Smith ME, Dupree R, Watts A
We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O--WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply...
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[NMR paper] NMR spectroscopy tools for structure-aided drug design.
NMR spectroscopy tools for structure-aided drug design.
Related Articles NMR spectroscopy tools for structure-aided drug design.
Angew Chem Int Ed Engl. 2004 Jan 3;43(3):290-300
Authors: Homans SW
Biomolecular NMR spectroscopy has expanded dramatically in recent years and is now a powerful tool for the study of structure, dynamics, and interactions of biomolecules. Previous limitations with respect to molecular size are no longer a primary barrier, and systems as large as 900 kDa were recently studied. NMR spectroscopy is already...
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11-24-2010 09:25 PM
[NMR paper] The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of p
The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.
Related Articles The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.
Annu Rev Biophys Biomol Struct. 1998;27:357-406
Authors: Gardner KH, Kay LE
During the past thirty years, deuterium labeling has been used to improve the resolution and sensitivity of protein NMR spectra used in a wide variety of applications. Most recently, the combination of triple resonance experiments and 2H, 13C, 15N labeled samples has...
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Restriction Endonucleases tools
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restriction endonucleases Double Digests table
Double Digest Finder
Cleavage Close to the End of DNA Fragments (oligonucleotides)
(2)H NMR study of the water dynamics in hydrated myoglobin.
(2)H NMR study of the water dynamics in hydrated myoglobin.
Related Articles (2)H NMR study of the water dynamics in hydrated myoglobin.
J Phys Chem B. 2010 Aug 12;114(31):10209-16
Authors: Lusceac SA, Vogel M
We use 1D and 2D (2)H NMR to study the temperature-dependent mechanism for the rotational motion of myoglobin hydration water. The results show that isotropic and anisotropic water reorientation is observed at high and low temperatures, respectively, with a continuous crossover in the temperature range of 200-230 K. The anisotropic...
Novel NMR tools to study structure and dynamics of biomembranes.
Linear Mode
