
Wednesday November 28, at 14:00, Kemicentrum Lecture hall B
Dr. Jens Nielsen, Univeristy College Dublin
The protonation states of protein residues governs the pH-dependence of
protein characteristics such as stability, binding energy and catalytic
efficiency. The protonation state of a titratable protein residue is
influenced by largely pH-independent terms such as desolvation and
interactions with permanent dipoles, but also with the pH-dependent
electrostatic interaction with other titratable residues.
In the lecture I will present two methods for determining electrostatic
interaction energies in proteins, and demonstrate how we can use these
methods to gain information on the dielectric constant of proteins.
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Last updated: 2007-11-27