Related ArticlesRecommendations 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 Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K
The recommendations presented here are designed to support easier communication of NMR data and NMR structures of proteins and nucleic acids through unified nomenclature and reporting standards. Much of this document pertains to the reporting of data in journal articles; however, in the interest of the future development of structural biology, it is desirable that the bulk of the reported information be stored in computer-accessible form and be freely accessible to the scientific community in standardized formats for data exchange. These recommendations stem from an IUPAC-IUBMB-IUPAB inter-union venture with the direct involvement of ICSU and CODATA. The Task Group has reviewed previous formal recommendations and has extended them in the light of more recent developments in the field of biomolecular NMR spectroscopy. Drafts of the recommendations presented here have been examined critically by more than 50 specialists in the field and have gone through two rounds of extensive modification to incorporate suggestions and criticisms.
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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Measurement of 1Hâ??15N and 1Hâ??13C residual dipolar couplings in nucleic acids from TROSY intensities
Measurement of 1Hâ??15N and 1Hâ??13C residual dipolar couplings in nucleic acids from TROSY intensities
Abstract Analogous to the recently introduced ARTSY method for measurement of one-bond 1Hâ??15N residual dipolar couplings (RDCs) in large perdeuterated proteins, we introduce methods for measurement of base 13Câ??1H and 15Nâ??1H RDCs in protonated nucleic acids. Measurements are based on quantitative analysis of intensities in 1Hâ??15N and 13Câ??1H TROSY-HSQC spectra, and are illustrated for a 71-nucleotide adenine riboswitch. Results compare favorably with those of conventional...
[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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[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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Use of chemical shifts for structural studies of nucleic acids
Use of chemical shifts for structural studies of nucleic acids
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 1 February 2010</br>
Sik Lok, Lam , Lai Man, Chi</br>
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Recommendations for the presentation of NMR structures of proteins and nucleic acids-
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