Описание:

ЯМР Программное обеспечение

The Dynamics Center is an easy-to-use and integrated platform featuring general dynamics and protein dynamics. It offers intuitive, method oriented workflows for the analysis of a wide range of experiments. All methods include components for sample description, data selection, analysis, result viewing, report (pdf) generation and export (text, EXCEL) functions. User input is minimized if experiments are performed with Bruker pulse programs. Multiple parallel execution of different methods is straightforward. The software is available for Windows, Linux and Mac systems. The software can be downloaded from www.bruker.com/de/service/support-upgrades/software-downloads/nmr.html. Tutorials including training data are available there as well.

The general dynamics application area currently supports relaxation (T1, T2, T1rho), Diffusion, Kinetics, Cross Polarization and REDOR data. Included are peak analysis, integration techniques, curve fitting, error analysis of integrals and fitted parameters by covariance analysis or Monte Carlo simulations. Details of the result viewing, report and export are configured by the user. The analysis also includes Inverse Laplace (ILT) techniques and Dosy plots. Supported data formats are 1D, pseudo 2D, 2D and pseudo 3D. Semi- and full automation is possible, especially for diffusion data.

Of particular interest is the analysis of kinetics data. Due to the nature of the samples, the spectra may show characteristic features such as resonance shifts, changes in line shapes, disappearing or evolving peaks. A newly developed peak tracker is able to handle these cases. The analysis includes fitting of up to 12 functions with automated model selection. The display of reaction profiles can be customized in various ways. The import of external profiles, e.g. based on IR data, allows the comparison of different experimental methods.

The protein dynamics application area offers the functionality of the former Protein Dynamics Center. The basic analysis includes 1H NOEsat./NOEunsat., 15N T1, T2, T1rho and Rex data and yields relaxation parameters. The modeling of dynamical parameters of protein backbones such as correlation times and order parameters is performed using reduced spectral density analysis and model free modeling. If the molecular structure is available, determination of the diffusion tensor and anisotropic modeling can be done. Also included is side chain modeling based on fractionally deuterated methyl groups as well as NOE build up analysis to get inter-nuclear distances.