MTMDAT
Automated analysis and visualisation of mass spectrometry data for tertiary and quaternary structure probing of proteins
This software has been developed by Klaus Hennig (Berlin, Germany) and Janosch Hennig. It facilitates fast and detailed evaluation of mass spectrometry data of limited proteolysis experiments to probe the tertiary structure of proteins and even complex formation with other proteins, ligands, and surfaces. Domain arrangements can be probed as well as stability on residue level.
The results can be plotted as time-course profiles, where degradation of unstable or accumulation of stable peptide fragments can be visualised, or as a 3D view (see figure) where the relative cleavage propensities of each cleavage site are displayed. For more information on the theoretical background you can check the publications and references therein.
As of January 2009 we have a new version (2.30.5) including e.g. a useful undo-function during peak assignment.The program is free (for academic/non-commercial purposes only) and can be downloaded by clicking on the link below (two links, one for windows and one fur unix-based machines), including a manual and example files. Please read the license agreement below and send it back signed to the address given below, especially if you want to have help.
Send it to: janhe@ifm.liu.se
or fax to: 004613-281399 (please notify by e-mail that you sent a fax)
snailmail: Janosch Hennig
IFM/Kemi - Linköping University
Campus Valla, Hus B
SE-581 83
Sweden
If you used MTMDAT in your research, please cite the following:
Hennig, J., Hennig, K.D., and Sunnerhagen, M., (2008), MTMDAT: Automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins. Bioinformatics, 24(10):1310-312.
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3D view of limited proteolysis data, analysed with mass spectrometry and evaluated by MTMDAT
