Fig. 2 Side chain dynamics obtained from deuterium T1 and T1ρ relaxation rates, see e.g. Clarkson MW and Lee AL, Biochemistry (2004) 43, 12448-12458.

Summary�� Easy to use interface�� Automated optimizations and setup�� Parameter reporting�� Fully automated processing up to 3D spectra

(including pseudo3D and NUS)�� Automated analysis of relaxation experiments

using the Dynamics Center

BioNMR Made Easy - bioTop

Biomolecular NMR, especially in case of proteins, can now be almost completely automated, from experiment selection to final processed spectra, including optimization of commonly used parameters.

bioTop will perform most of the everyday tasks in full automation. Minimal user interaction is required for most experiments. It can be used right after inserting the sample and will take care of shimming, locking and tuning if necessary.

Experiment SelectionExperiments can be added from an intuitive interface. Once selected, a dataset is prepared and set-up, ready for acquisition. At this stage the user can edit individual parameters from a very simple dialogue.

To keep full flexibility, the ability to edit the prepared datasets in Topspin in the usual way is kept and does not interfere with bioTop functionalities.

Automate ProcessingCurrently, processing of spectra up to three dimensions is supported, including pseudo3D spectra, non-uniform sampling, and raw data splitting where needed. If Dynamics Center is available, an appropriate default analysis will be performed for relaxation measurements, also fully automated.

Parameter OptimizationsCommonly used experimental parameters can be edited by the experienced user or be marked for optimization, this however can be omitted completely. In this case the program will suggest optimizations based on experiments selected.

Fig. 2: Parameter optimizations section. Parameters which are usually shared by a number of experiments can be optimized without human intervention, including offsets, spectral widths and almost all parameters related to water suppression. It is also possible to import optimized parameters from previous runs or report to a pdf.

Fig. 3: Example report, created after all optimizations have been performed.

Fig. 1: Sample information tab. Entered descriptions will be used for reporting. Labeling and solvent will be used to filter the suitable experiments list, as well as for the selection of appropriate optimization experiments, together with the molecular size.

Fig. 5: 3D BEST HNCACB of ubiquitin using NUS. Processed automatically including phase correction and strip transformation.

CustomizationThe users can create their own user-defined sections of experiments. This can be used to restructure the existing experiments into different groups, create presets as well as adding your own parameter sets and pulse programs. As long as the experiments are prosol compatible, they can be included.

Fig. 4: Experiments tab. From a list of available experiments, either individual or multiple experiments can be transferred to a to-do list. A right click on the right hand list will provide a menu with dataset operations based on the current status of the experiment, including automated processing once acquisition is finished.