e:mail jens@jens-meiler.de
VORDIPLOM (equivalent to B.Sc.) in Chemistry,
University of Leipzig, Germany, 1995
DIPLOM (equivalent to M.Sc.) in Chemistry,
University of Leipzig, Germany, 1998
Ph.D. in Chemistry, University of Frankfurt, Germany, 2001
Postdoctoral Fellow, University of Washington,
Seattle, USA, with Prof. David Baker. 2001-2005
Assistant Professor, Vanderbilt University,
Center for Structural Biology, Departments of
Chemistry and Pharmacology. 2005-
Áreas de interés:
Conferencia
Prediction and design of protein structures
Resumen
Rosetta predictions in the Fifth and Sixth
Community-Wide Experiment on the Critical Assessment
of Techniques for Protein Structure Prediction
(CASP) are presented, focusing on the free modeling
category. The application of this prediction technique
for rapid protein fold elucidation from unassigned NMR
spectra is illustrated. NMR spectroscopy has the advantage
of rapidly providing the structurally relevant information in
the form of unassigned chemical shifts (CSs), intensities
of NOESY crosspeaks [nuclear Overhauser effects (NOEs)], and
residual dipolar couplings (RDCs). We developed a method for generating
low-resolution protein structures by using unassigned NMR data that
relies on de novo protein structure prediction algorithm and Monte Carlo
procedure that searches for the assignment of resonances
to atoms that produces the best fit of the experimental NMR
data to a candidate 3D structure. Protein small molecule docking
algorithms provide a means to elucidate the interface of presently
unknown protein small molecule complexes in structural detail.
Here I present and evaluate a new method that docks a rigid-body
small molecules into protein binding sites employing a simultaneous
Monte-Carlo search for position, orientation, and protein
sidechain conformation.
In the last part of this presentation protein design algorithms are
discussed on the example of the de novo designed protein fold of TOP7.
This method was expanded on the design of protein-ligand interfaces.