Regensburg 2010 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 28: Poster: Biopolymers and Biomaterials
CPP 28.9: Poster
Wednesday, March 24, 2010, 17:30–19:00, Poster C
AUREMOL: Automatic protein structure determination from NMR data — •Harald Donaubauer1, Tobias Harsch1, Willhelm Malloni1, Silivia de Sanctis1, Bärbel Kieninger1, Nina Danilova1, Konrad Brunner1, Wolfram Gronwald1, Jochen Trenner1, Klaus-Peter Neidig2, and Hans-Robert Kalbitzer1 — 1University of Regensburg — 2Bruker BioSpin
Several approaches to the problem of automated protein structure determination from NMR data exist. The concept for automation is a molecule centred approach where all of the available a priori information is used to eliminate as many free parameters as possible and reduce the amount of information and experimental data. Using a starting structure and as much additional information as possible, like predicted chemical shifts and backbone torsion angles, the assignment and the structure itself are refined in an iterative process. Therefore we are developing AUREMOL, which goal is the reliable and automatic structure determination of biological macro molecules such as proteins from NMR data(1). In AUREMOL included modules are RELAX, which uses complete relaxation formalism to calculate a simulated NOESY NMR spectrum, SIBASA (simulated based sequential assignment), which bases on simulated annealing to determine the chemical shifts of these signals, KNOWNOE, REFINE, which calculates intermolecular distances from a NOESY spectrum and the structure evaluation RFAC. (1)Gronwald, W. and Kalbitzer, H.R. Automated Structure Determination of Proteins by NMR Spectroscopy. 2004, Progr. NMR Spectr. 44, 33-96