caa a22 4500 445325968 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10858-011-9509-1 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9509-1 relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins [Elektronische Daten] [Michael Bieri, Edward d'Auvergne, Paul Gooley] Investigation of protein dynamics on the ps-ns and μs-ms timeframes provides detailed insight into the mechanisms of enzymes and the binding properties of proteins. Nuclear magnetic resonance (NMR) is an excellent tool for studying protein dynamics at atomic resolution. Analysis of relaxation data using model-free analysis can be a tedious and time consuming process, which requires good knowledge of scripting procedures. The software relaxGUI was developed for fast and simple model-free analysis and is fully integrated into the software package relax. It is written in Python and uses wxPython to build the graphical user interface (GUI) for maximum performance and multi-platform use. This software allows the analysis of NMR relaxation data with ease and the generation of publication quality graphs as well as color coded images of molecular structures. The interface is designed for simple data analysis and management. The software was tested and validated against the command line version of relax. Springer Science+Business Media B.V., 2011 Graphical user interface nationallicence GUI nationallicence Lipari and Szabo model-free analysis nationallicence NMR spin relaxation nationallicence Protein dynamics nationallicence Relax software nationallicence CSA : Chemical shift anisotropy nationallicence GUI : Graphical user interface nationallicence HSQC : Heteronuclear single quantum coherence nationallicence OMP : Olfactory marker protein nationallicence NOE : Nuclear overhauser effect nationallicence R ex : Chemical exchange relaxation nationallicence Bieri Michael Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 3010, Parkville, VIC, Australia aut d'Auvergne Edward Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Goettingen, Germany aut Gooley Paul Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 3010, Parkville, VIC, Australia aut Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 147-155 0925-2738 50:2<147 2011 50 10858 https://doi.org/10.1007/s10858-011-9509-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9509-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Bieri Michael Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 3010, Parkville, VIC, Australia aut NATIONALLICENCE 700 1- d'Auvergne Edward Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Goettingen, Germany aut NATIONALLICENCE 700 1- Gooley Paul Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 3010, Parkville, VIC, Australia aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 147-155 0925-2738 50:2<147 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer