Berlin 2005 – scientific programme

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AKB: Biologische Physik

AKB 100: Poster Session I

AKB 100.57: Poster

Saturday, March 5, 2005, 16:45–18:45, Poster TU D

Φ-values and Transition States in Protein Folding — •Claudia Merlo and Thomas R. Weikl — Max Planck Institute of Colloids and Interfaces, Theory Division, 14424 Potsdam

Small single-domain proteins typically are two-state folders, i.e. they fold from the denatured to the native state without populating experimentally detectable intermediate states. The folding kinetics of two-state folders usually is explored through mutational Φ-value analysis. Φ-values are experimental measures of how the kinetics of protein folding is changed by single-site mutations. Φ-values measure energetic quantities, but are often interpreted in terms of the structures of the transition state ensemble. Here we present a simple analytical model of folding kinetics in terms of the formation of protein substructures. The model shows that Φ-values have both structural and energetic components. It thus provides a natural and general interpretation of Φ-values, including so-called “nonclassical" Φ-values less than zero or larger than one.