|
CURRENT
RESEARCH IN OUR GROUP
|
 |
 |
 |
|
FORCE FIELDS |
DFT
METHODS |
MOLECULAR EVOLUTION |
|
Electrostatic
interactions dominate the structure and free energy
of biomolecules. Current force fields
display large errors in relative free energies of
charged groups, including metal ions, halide ions,
and charged amino acid side chains.
We attempt to remedy this by
developing new force field parameters that are
consistent, i.e. on the
same free-energy scale. |
The main theoretical
method used in today's chemistry is DFT. We use
accurate benchmarks to evaluate density functionals,
and to rationally explain why some functionals fail
and others succeed in modeling particular properties.
|
Our ultimate goal is
to understand molecular evolution all the way from
the detailed molecular structure, via the
corresponding function, and up to the psysiological
level.
We are currently mainly concerned with
metalloproteins such as O2-binding,
Fe-containing myoglobin and Cu-containing lacasses.
|
-
K. P. Jensen, W. L. Jorgensen,
-
"Halide, Ammonium, and Alkali Metal Ion
Parameters for Modeling Aqueous Solutions",
-
J. Chem. Theory. Comput. 2006, 2, 1499-1509.
-
K. P. Jensen,
-
"Improved Interaction Potentials for Charged
Residues in Proteins",
-
J. Phys. Chem. B 2008, 112, 1820-1827.
|
-
K.
P. Jensen*,
-
"Bioinorganic
Chemistry Modeled with the TPSSh Functional",
-
Inorg. Chem. 2008, 47, 10357-10365.
-
K. P. Jensen, B. O. Roos, U. Ryde,
-
"Performance
of Density Functionals for First Row Transition
Metals",
-
J. Chem. Phys. 2007, 126, 014103.
|
-
K. P. Jensen, P. Rydberg, J. Heimdal, U.
Ryde,
-
"A Comparison of Tetrapyrrole Cofactors in
Nature and their Tuning by Axial Ligands ",
-
in: "Computational Modeling for Homogenous
and Enzymatic Catalysis", Chapter 2, p. 27.
-
Ed.
D. G. Musaev and K. Morokuma, Wiley-VCH Verlag
GmbH & Co. 2008.
|
|
copyright 2008 k.p. kepp |
|