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Literature DB >> 20012760

S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments.

Petr Novák¹, Lukás Zídek, Veronika Motácková, Petr Padrta, Alzbeta Svenková, Jean-Marc Nuzillard, Libor Krásný, Vladimír Sklenár.

Abstract

S3EPY is a Python extension to the program Sparky written to facilitate the assessment of coupling constants from in-phase/antiphase and spin-state-selective excitation (S(3)E) experiments. It enables the routine use of small scalar couplings by automating the coupling evaluation procedure. S3EPY provides an integrated graphical user interface to programs which outputs graphs and the table of determined couplings.

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Year: 2009 PMID： 20012760 DOI： 10.1007/s10858-009-9392-1

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

13 in total

1. Internal consistency of NMR data obtained in partially aligned biomacromolecules.

Authors: Lukás Zídek; Petr Padrta; Josef Chmelík; Vladimír Sklenár
Journal: J Magn Reson Date: 2003-06 Impact factor: 2.229

2. Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants.

Authors: P Andersson; J Weigelt; G Otting
Journal: J Biomol NMR Date: 1998-10 Impact factor: 2.835

3. Integration of spin-state-selective excitation into 2D NMR correlation experiments with the heteronuclear ZQ/2Q pi rotations for 1JXH- resolved E.COSY-type measurements of heteronuclear coupling constants in proteins.

Authors: A Meissner; J O Duus; O W Sørensen
Journal: J Biomol NMR Date: 1997-07 Impact factor: 2.835

Review 4. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra.

Authors: M Ottiger; F Delaglio; A Bax
Journal: J Magn Reson Date: 1998-04 Impact factor: 2.229

5. Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra.

Authors: N Tjandra; A Bax
Journal: J Magn Reson Date: 1997-02 Impact factor: 2.229

1. Solution structure of domain 1.1 of the σ^A factor from Bacillus subtilis is preformed for binding to the RNA polymerase core.

Authors: Milan Zachrdla; Petr Padrta; Alžbeta Rabatinová; Hana Šanderová; Ivan Barvík; Libor Krásný; Lukáš Žídek
Journal: J Biol Chem Date: 2017-05-24 Impact factor: 5.157

1 in total

S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments.

1. Internal consistency of NMR data obtained in partially aligned biomacromolecules.

2. Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants.

3. Integration of spin-state-selective excitation into 2D NMR correlation experiments with the heteronuclear ZQ/2Q pi rotations for 1JXH- resolved E.COSY-type measurements of heteronuclear coupling constants in proteins.

Review 4. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra.

5. Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra.

6. Measurement of small scalar and dipolar couplings in purine and pyrimidine bases.

7. NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

8. Cloned gene encoding the delta subunit of Bacillus subtilis RNA polymerase.

9. Refinement of d(GCGAAGC) hairpin structure using one- and two-bond residual dipolar couplings.

10. Structure of Bombyx mori chemosensory protein 1 in solution.

1. Solution structure of domain 1.1 of the σ^A factor from Bacillus subtilis is preformed for binding to the RNA polymerase core.