Regensburg 2010 – scientific programme

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BP: Fachverband Biologische Physik

BP 34: Posters: New Technologies

BP 34.13: Poster

Thursday, March 25, 2010, 17:15–20:00, Poster B2

Fluorescence spectroscopic studies of protein conformational dynamics — •Phillip Kroehn — Drittes Physikalisches Institut, Georg August Universität Göttingen, Friedrich-Hund-Platz 1, 37077 Göttingen

Proteinfolding is the physical process by which a polypeptidechain folds into its functional three dimensional structure from a random coil.

The WW-domain is the smallest betasheet known. It consists of a lightly hydrophobic core and takes part in protein-protein interactions by binding of proline rich regions. By singlemolecule FRET studies we want to analyse the folding/unfolding dynamics of the WW-domain and its intermediate states. The unfolding of the protein will be accomplished by chemical or thermal denaturation.

To use smFRET we are going to label the WW-domain specifically with fluorophoric dyes by employing the orthogonal system. This new technique allows us to use a stopcodon as a codon for an unnatural aminoacid, like para-acetylphenylalanine, whereby it is placed in the polypeptidechain. We are able to specifically label these unnatural aminoacid in the protein.