Summary: The PMMB fellowship partially supported the development
of an effective energy function for proteins in solution (EEFl), which
includes an analytical model for the solvation free energy of a protein.
Modeling the solvent implicitly leads to dramatic savings in computer time
and allows the simulation of larger systems and for longer times. Furthermore,
it was shown that this function can discriminate the native from misfolded
protein conformations and, hence, could be of use in protein structure
prediction. It also allows us to study the denatured state of proteins
in solution. The results so far indicate that the denatured state at zero
denaturant concentration is compact and has higher heat capacity than the
native state not only because of increased solvent exposure of hydrophobic
groups but also because of the higher lability of the intraprotein interactions
in this compact state. |
