Related ArticlesHydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin.
The influence of hydration on the internal dynamics of a typical EF-hand calciprotein, parvalbumin, was investigated by incoherent quasi-elastic neutron scattering (IQNS) and solid-state 13C-NMR spectroscopy using the powdered protein at different hydration levels. Both approaches establish an increase in protein dynamics upon progressive hydration above a threshold that only corresponds to partial coverage of the protein surface by the water molecules. Selective motions are apparent by NMR in the 10-ns time scale at the level of the polar lysyl side chains (externally located), as well as of more internally located side chains (from Ala and Ile), whereas IQNS monitors diffusive motions of hydrogen atoms in the protein at time scales up to 20 ps. Hydration-induced dynamics at the level of the abundant lysyl residues mainly involve the ammonium extremity of the side chain, as shown by NMR. The combined results suggest that peripheral water-protein interactions influence the protein dynamics in a global manner. There is a progressive induction of mobility at increasing hydration from the periphery toward the protein interior. This study gives a microscopic view of the structural and dynamic events following the hydration of a globular protein.
Hydration dependent dynamics in RNA
Hydration dependent dynamics in RNA
Abstract The essential role played by local and collective motions in RNA function has led to a growing interest in the characterization of RNA dynamics. Recent investigations have revealed that even relatively simple RNAs experience complex motions over multiple time scales covering the entire msâ??ps motional range. In this work, we use deuterium solid-state NMR to systematically investigate motions in HIV-1 TAR RNA as a function of hydration. We probe dynamics at three uridine residues in different structural environments ranging from helical to...
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[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Related Articles Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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[NMR paper] NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
Related Articles NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
J Mol Biol. 2000 Oct 6;302(5):1101-17
Authors: Tsui V, Radhakrishnan I, Wright PE, Case DA
The hydration of a high-affinity protein-DNA complex involving the three amino terminal zinc finger domains of transcription factor IIIA (TFIIIA) and a 15-base-pair DNA duplex was investigated by NMR spectroscopy and molecular dynamics (MD) simulations. Intermolecular nuclear...
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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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Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
Related Articles Hydration water dynamics in biopolymers from NMR relaxation in the rotating frame.
J Magn Reson. 2010 Sep 24;
Authors: Blicharska B, Peemoeller H, Witek M
Assuming dipole-dipole interaction as the dominant relaxation mechanism of protons of water molecules adsorbed onto macromolecule (biopolymer) surfaces we have been able to model the dependences of relaxation rates on temperature and frequency. For adsorbed water molecules the correlation times are...
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[NMR paper] The influence of hydration on the conformation of bovine serum albumin studied by sol
The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C-NMR spectroscopy.
Related Articles The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C-NMR spectroscopy.
Biopolymers. 1993 Dec;33(12):1871-6
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton-decoupled cross-polarization magic-angle spinning nmr spectra of bovine serum albumin are reported as a function of hydration. Increases in hydration level enhance the resolution of the peak centered at...
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[NMR paper] The influence of hydration on the conformation of lysozyme studied by solid-state 13C
The influence of hydration on the conformation of lysozyme studied by solid-state 13C-NMR spectroscopy.
Related Articles The influence of hydration on the conformation of lysozyme studied by solid-state 13C-NMR spectroscopy.
Biopolymers. 1993 Apr;33(4):513-9
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton decoupled cross-polarization magic-angle spinning nmr spectra of lysozyme are reported as a function of hydration. Increases in hydration level enhance the resolution of the spectra, particularly in the aliphatic region, but has no...
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[NMR paper] Protein hydration studied with homonuclear 3D 1H NMR experiments.
Protein hydration studied with homonuclear 3D 1H NMR experiments.
Related Articles Protein hydration studied with homonuclear 3D 1H NMR experiments.
J Biomol NMR. 1991 Jul;1(2):209-15
Authors: Otting G, Liepinsh E, Farmer BT, Wüthrich K
Homonuclear 3D 1H NOESY-TOCSY and 3D 1H ROESY-TOCSY experiments were used to resolve and assign nuclear Overhauser effect (NOE) cross peaks between the water signal and individual polypeptide proton resonances in H2O solutions of the basic pancreatic trypsin inhibitor. Combined with a novel, robust...
Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the cas
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