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BP: Fachverband Biologische Physik

BP 8: Posters: Proteins

BP 8.13: Poster

Montag, 11. März 2013, 17:30–19:30, Poster B2

Proteinfoldingdynamics of hPin1 WW domain studied by single molecule FRET. — •Phillip Kroehn and Jörg Enderlein — Universität Göttingen, Deutschland

Georg-August-Universität Göttingen, Friedrich-Hundt-Platz 1, 37077 Göttingen

Förster resonance energy transfer (FRET) is the commonly used method to study fast molecular dynamics in a scale of 1-10 nanometer.

The energy transfer between a donor molecule and an acceptor molecule e.g. organic fluorophore by dipole interaction depends strongly on the distance between them.This phenomenon offers the possibility to use FRET as a nonoscopic ruler.

The primary structure of small soluble proteins is believed to contain all chemical information necessary for proper folding to its native state.The hPin1 WW Domain is a 40 Amino acid all beta sheet protein that consist of three strands. It can be seen as a simple model system to investigate the formation of beta fold secondary structures.

The hPin1 is involved in cell cycle regulation, the WW domain at the N terminal site of hPin1 is able to bind to proline rich ligands. Due to its high thermal stability the hPin1 WW domain is suitable for folding/unfolding studies.