Berlin 2008 – scientific programme

Parts | Days | Selection | Search | Downloads | Help

BP: Fachverband Biologische Physik

BP 25: Protein Structure and Folding

BP 25.1: Talk

Thursday, February 28, 2008, 14:30–14:45, PC 203

Transition states in protein folding — •Thomas Weikl — Max-Planck-Institut für Kolloid- und Grenzflächenforschung, Abteilung Theorie und Bio-Systeme, Wissenschaftspark Golm, 14424 Potsdam

Conformational transitions of proteins are often apparent two-state processes. Examples are the folding and unfolding of small single-domain proteins, or the opening and closing of ion channels. The dynamics of two-state processes is thought to be governed by a transition-state barrier between the two states. Transition states are short-lived and cannot be observed directly in experiments. However, a mutational analysis of the two-state dynamics can provide indirect access. In a mutational analysis, experimentalists measure the effect of point mutations on the folding and unfolding rates of small proteins, or the opening and closing rates of ion channels. I will present models that help to reconstruct folding transition states from mutational data. The models are based on identifying cooperative substructural elements of proteins, and on calculating mutation-induced free-energy changes for these elements.

References:

[1] C. Merlo, K. A. Dill, and T. R. Weikl, PNAS 102, 10171 (2005).

[2] T. R. Weikl and K. A. Dill, J. Mol. Biol. 365, 1578 (2007).

[3] T. R. Weikl, Biophys. J., in press (2008).