Abstract We observed and characterized two distinct signals originating from different pools of water protons in solid-state NMR protein samples, namely from crystal water which exchanges polarization with the protein (on the NMR timescale) and is located in the protein-rich fraction at the periphery of the magic-angle spinning (MAS) sample container, and supernatant water located close to the axis of the sample container. The polarization transfer between the water and the protein can be probed by two-dimensional exchange spectroscopy, and we show that the supernatant water does not interact with protein on the timescale of the experiments. The two water pools have different spectroscopic properties, including resonance frequency, longitudinal, transverse and rotating frame relaxation times. The supernatant water can be removed almost completely physically or can be frozen selectively. Both measures lead to an enhancement of the quality factor of the probe circuit, accompanied by an improvement of the experimental signal/noise, and greatly simplify solvent-suppression by substantially reducing the water signal. We also present a tool, which allows filling solid-state NMR sample containers in a more efficient manner, greatly reducing the amount of supernatant water and maximizing signal/noise.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
J Magn Reson. 2011 Jul 6;
Authors: Yin Y, Nevzorov AA
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up...
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Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011</br>
Yuanyuan, Yin , Alexander A., Nevzorov</br>
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up structural...
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06-21-2011 03:40 PM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
[NMR paper] Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Related Articles Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Biophys J. 2005 Oct;89(4):2792-805
Authors: Rainey JK, Sykes BD
Sample orientation relative to the static magnetic field of an NMR spectrometer allows study of membrane proteins in the lipid bilayer setting. The straightforward preparation and handling of extremely thin mica substrates with consistent surface properties has prompted us to examine oriented phospholipid...
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[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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11-24-2010 09:16 PM
[NMR paper] Preparation of protein nanocrystals and their characterization by solid state NMR.
Preparation of protein nanocrystals and their characterization by solid state NMR.
Related Articles Preparation of protein nanocrystals and their characterization by solid state NMR.
J Magn Reson. 2003 Nov;165(1):162-74
Authors: Martin RW, Zilm KW
Preparation of proteins in their crystalline state has been found to be important in producing stable therapeutic protein formulations, cross-linked enzyme crystals for application in industrial processes, generating novel porous media for separations, and of course in structure elucidation. Of these...
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[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...
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08-21-2010 11:12 PM
[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...
Characterization of different water pools in solid-state NMR protein samples
Linear Mode
