Publication year: 2010 Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 1 February 2010
Sik Lok, Lam , Lai Man, Chi
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Abstract Unravelling the complex correlation between chemical shifts of 13 C α, 13 C β, 13 C�, 1 H α, 15 N, 1 H N atoms in amino acids of proteins from NMR experiment and local structural environments of amino acids facilitates the assignment of secondary structures of proteins. This is an important impetus for both determining the three-dimensional structure and understanding the biological function of proteins. The previous...
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[NMR paper] Secondary structural effects on protein NMR chemical shifts.
Secondary structural effects on protein NMR chemical shifts.
Related Articles Secondary structural effects on protein NMR chemical shifts.
J Biomol NMR. 2004 Nov;30(3):233-44
Authors: Wang Y
For an amino acid in protein, its chemical shift, delta(phi, psi)(s), is expressed as a function of its backbone torsion angles (phi and psi) and secondary state (s): delta(phi, psi)(s=deltaphi, psi)_coil+Deltadelta(phi, psi)_s), where delta(phi, psi)(coil) represents its chemical shift at coil state (s=coil); Delta delta(phi, psi)(s) (s=sheet or helix) is...
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11-24-2010 10:03 PM
[NMR paper] Recommendations for the presentation of NMR structures of proteins and nucleic acids-
Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy.
Related Articles Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy.
Eur J Biochem. 1998 Aug 15;256(1):1-15
Authors: Markley JL, Bax A, Arata...
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11-17-2010 11:15 PM
[NMR paper] Recommendations for the presentation of NMR structures of proteins and nucleic acids.
Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy.
Related Articles Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy.
J Biomol NMR. 1998 Jul;12(1):1-23
Authors: Markley JL, Bax A, Arata Y,...
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[NMR paper] Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P N
Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P NMR.
Related Articles Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P NMR.
J Biochem. 1994 Feb;115(2):270-8
Authors: Odahara T, Nishimoto S, Katsutani N, Kyogoku Y, Morimoto Y, Matsushiro A, Akutsu H
The dynamic properties of nucleic acids in five different types of intact supramolecular systems, namely, chicken erythrocyte chromatin, the wild type and a deletion mutant of the lambda phage, lipid-containing phage PM2, and...
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08-22-2010 03:33 AM
[NMR paper] Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P N
Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P NMR.
Related Articles Dynamic properties of nucleic acids in biosupramolecular systems, as studied by 31P NMR.
J Biochem. 1994 Feb;115(2):270-8
Authors: Odahara T, Nishimoto S, Katsutani N, Kyogoku Y, Morimoto Y, Matsushiro A, Akutsu H
The dynamic properties of nucleic acids in five different types of intact supramolecular systems, namely, chicken erythrocyte chromatin, the wild type and a deletion mutant of the lambda phage, lipid-containing phage PM2, and...
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08-22-2010 03:33 AM
Mapping of protein structural ensembles by chemical shifts
Abstract Applying the chemical shift prediction programs SHIFTX and SHIFTS to a data base of protein structures with known chemical shifts we show that the averaged chemical shifts predicted from the structural ensembles explain better the experimental data than the lowest energy structures. This is in agreement with the fact that proteins in solution occur in multiple conformational states in fast exchange on the chemical shift time scale. However, in contrast to the real conditions in solution at ambient temperatures, the standard NMR structural calculation methods as well chemical shift...
Use of chemical shifts for structural studies of nucleic acids
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