Related ArticlesDetection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.
J Biomol NMR. 2005 Apr;31(4):295-310
Authors: Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B
Water molecules are a major determinant of protein stability and are important for understanding protein-protein interactions. We present two experiments which allow to measure first the effective T(2) decay rate of individual amide proton, and second the magnetization build-up rates for a selective transfer from H(2)O to H(N) using spin diffusion as a mixing element. The experiments are demonstrated for a uniformly (2)H, (15)N labeled sample of a microcrystalline SH3 domain in which exchangeable deuterons were back-substituted with protons. In order to evaluate the NMR experimental data, as X-ray structure of the protein was determined using the same crystallization protocol as for the solid-state NMR sample. The NMR experimental data are correlated with the dipolar couplings calculated from H(2)O-H(N) distances which were extracted from the X-ray structure of the protein. We find that the H(N) T(2) decay rates and H(2)O-H(N) build-up rates are sensitive to distance and dynamics of the detected water molecules with respect to the protein. We show that qualitative information about localization and dynamics of internal water molecules can be obtained in the solid-state by interpretation of the spin dynamics of a reporter amide proton.
[NMR paper] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR
Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 5;125(44):13336-7
Authors: Lesage A, Böckmann A
Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...
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[NMR paper] A high-resolution NMR study of long-lived water molecules in both oxidation states of
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Related Articles A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Biochemistry. 2003 Apr 1;42(12):3457-63
Authors: Bertini I, Ghosh K, Rosato A, Vasos PR
The interaction of water with oxidized and reduced cytochrome c from the Gram-positive bacterium Bacillus pasteurii (a 71-amino acid long monoheme cytochrome) is investigated through CLEANEX experiments and (15)N-edited...
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[NMR paper] Protein hydration and location of water molecules in oxidized horse heart cytochrome
Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
Related Articles Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
J Magn Reson. 2000 Nov;147(1):1-8
Authors: Bertini I, Huber JG, Luchinat C, Piccioli M
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by (1)H NMR spectroscopy. Two-dimensional, homonuclear ePHOGSY-NOESY experiments are used to map water-protein interactions. The detected NOEs reveal...
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[NMR paper] Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solu
Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solution measured by NMR spectroscopy.
Related Articles Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solution measured by NMR spectroscopy.
J Mol Biol. 1998 Oct 2;282(4):847-58
Authors: Sunnerhagen M, Denisov VP, Venu K, Bonvin AM, Carey J, Halle B, Otting G
The present NMR study investigates the residence times of the hydration water molecules associated with uncomplexed trp operator DNA in solution by measuring intermolecular...
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[NMR paper] Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in
Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
Related Articles Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
J Biomol NMR. 1998 Jan;11(1):1-15
Authors: Pfeiffer S, Spitzner N, Löhr F, Rüterjans H
The hydration of uncomplexed RNase T1 was investigated by NMR spectroscopy at pH 5.5 and 313 K. Two-dimensional heteronuclear NOE and ROE difference experiments were employed to determine the spatial proximity and the residence times of water molecules at...
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[NMR paper] Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by
Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
Biochemistry. 1996 Oct 1;35(39):12694-704
Authors: Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN
A tetrahedrally hydrogen-bonded structural water molecule, water 301, is seen in...
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[NMR paper] Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Related Articles Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
J Biomol NMR. 1995 Jun;5(4):415-9
Authors: Cistola DP, Hall KB
A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines 19F-detected heteronuclear Overhauser and exchange spectroscopy (HOESY) with site-specific 19F substitution. The model system employed was intestinal fatty acid-binding protein complexed with...
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[NMR paper] Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lyso
Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lysozyme and trapped in a lysozyme-inhibitor complex.
Related Articles Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lysozyme and trapped in a lysozyme-inhibitor complex.
Biophys Chem. 1999 Mar 29;77(2-3):111-21
Authors: Baguet E, Hennebert N
Triple-quantum filtering NMR sequences were used to study the multiexponential relaxation behaviour of H2 17O in the presence of hen egg white lysozyme. By this means, the fraction and the...