Related ArticlesThe (17)O-NMR shielding range and shielding time scale and detection of discrete hydrogen-bonded conformational states in peptides.
Biopolymers. 2001 Sep;59(3):125-30
Authors: Gerothanassis IP
The (17)O-NMR shielding range and shielding time scale due to hydrogen-bonding interactions in peptides are critically evaluated relative to those of (1)H-NMR. Furthermore, the assumptions and conclusions in previous (17)O-NMR studies on the detection of discrete conformational states in peptides (V. Tsikaris et al., Biopolymers, 2000, Vol. 53, pp. 135-139) are reconsidered. Consistent examination of the method demonstrates that although (17)O shieldings of peptide oxygens are very sensitive to hydrogen bonding interactions, the (17)O-NMR shielding time scale is not advantageous compared to that of (1)H-NMR, and thus it is not suitable for the detection of discrete hydrogen-bonded conformational states in peptides. (17)O-NMR spectroscopy is prone to interpretation errors due to the formation of (17)O-labeled impurities during the synthetic procedures (A. Steinschneider et al., International Journal of Peptide and Protein Research, 1981, Vol. 18, pp. 324-333).
Investigation of solvent effect and NMR shielding tensors of p53 tumor-suppressor gene in drug design.
Investigation of solvent effect and NMR shielding tensors of p53 tumor-suppressor gene in drug design.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Investigation of solvent effect and NMR shielding tensors of p53 tumor-suppressor gene in drug design.
Int J Nanomedicine. 2011;6:213-8
Authors: Irani S, Monajjemi M, Honarparvar B, Atyabi S, Sadeghizadeh M
Abstract
The p53 tumor-suppressor gene encodes a nuclear phosphoprotein with cancer- inhibiting properties. The...
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Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Abstract We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3....
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[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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11-19-2010 08:32 PM
[NMR paper] Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
Related Articles Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
J Biomol Struct Dyn. 1999 Aug;17(1):157-74
Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies...
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11-18-2010 08:31 PM
Conformational dependence of 13C shielding and coupling constants for methionine
Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...
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08-25-2010 03:51 PM
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Si
Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
Related Articles Microsecond Time Scale Mobility in a Solid Protein As Studied by the (15)N R(1rho) Site-Specific NMR Relaxation Rates.
J Am Chem Soc. 2010 Aug 6;
Authors: Krushelnitsky A, Zinkevich T, Reichert D, Chevelkov V, Reif B
For the first time, we have demonstrated the site-resolved measurement of reliable (i.e., free of interfering effects) (15)N R(1rho) relaxation rates from a solid protein to extract dynamic...
Monitoring H-D exchange on second time scale with Frydman NMR spectroscopy
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Real-Time Monitoring of Chemical Transformations by Ultrafast 2D NMR Spectroscopy
Maayan Gal, Mor Mishkovsky, and Lucio Frydman
J. Am. Chem. Soc.; 2006; 128(3) pp 951 - 956;
Abstract:
The (17)O-NMR shielding range and shielding time scale and detection of discrete hydr
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