Site-resolved measurement of water-protein interactions by solution NMR.
Nat Struct Mol Biol. 2011 Jan 2;
Authors: Nucci NV, Pometun MS, Wand AJ
The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confining proteins within the nanoscale interior of a reverse micelle slows water dynamics, allowing global protein-water interactions to be detected using nuclear magnetic resonance techniques. Complications that normally arise from hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle medium. Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of nuclear Overhauser effects obtained in the laboratory and rotating frames indicate a considerable range of hydration water dynamics is present on the protein surface. In addition, an unprecedented clustering of different hydration-dynamics classes of sites is evident.
PMID: 21196937 [PubMed - as supplied by publisher]
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
Abstract Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through...
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A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR. 2011 May 29;
Authors: Amero C, Asunción Durá M, Noirclerc-Savoye M, Perollier A, Gallet B, Plevin MJ, Vernet T, Franzetti B, Boisbouvier J
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance...
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06-01-2011 02:30 PM
[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] Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by N
Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
Related Articles Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
J Biomol NMR. 2001 Jun;20(2):111-26
Authors: Gruschus JM, Ferretti JA
Hydration site lifetimes of slowly diffusing water molecules at the protein/DNA interface of the vnd/NK-2 homeodomain DNA complex were determined using novel three-dimensional NMR techniques. The lifetimes were calculated using the ratios of ROE and NOE cross-relaxation rates between...
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11-19-2010 08:32 PM
[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM
Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Protein Sci. 2000 Aug;9(8):1540-7
Authors: Kutyshenko VP, Cortijo M
We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...
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[NMR paper] Solution NMR characterization of hydrogen bonds in a protein by indirect measurement
Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
J Magn Reson. 1997 Jul;127(1):54-64
Authors: Liwang AC, Bax A
Hydrogen bonds stabilize protein and nucleic acid structure, but little direct spectroscopic data have been available for...
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08-22-2010 03:31 PM
[NMR paper] Solution NMR characterization of hydrogen bonds in a protein by indirect measurement
Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
J Magn Reson. 1997 Jul;127(1):54-64
Authors: Liwang AC, Bax A
Hydrogen bonds stabilize protein and nucleic acid structure, but little direct spectroscopic data have been available for...
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08-22-2010 03:03 PM
[NMR paper] Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,
Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Related Articles Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Adv Exp Med Biol. 1991;302:541-60
Authors: Kumosinski TF, Pessen H, Farrell HM
The importance of water interactions with proteins in food systems is well documented. A controversy exists, however, as to the nature of these interactions and the effect of protein structural...
Site-resolved measurement of water-protein interactions by solution NMR.
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