Related ArticlesProbing 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 [2-mono-19F]-palmitate. An intense cross peak was observed between the fluorine and a buried water molecule, as defined in the 1.98 A crystal structure of the complex. From HOESY spectra, the fluorine-water distance was estimated to be 2.1 A, in agreement with the crystal structure. This approach may be applicable to macromolecules that are too large for 1H-detected NMR methods.
[NMR paper] Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain o
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.
Related Articles Detection 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...
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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] Identification and localization of bound internal water in the solution structure of
Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy.
Related Articles Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy.
Biochemistry. 1990 Jun 19;29(24):5671-6
Authors: Clore GM, Bax A, Wingfield PT, Gronenborn AM
...
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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...
Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
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