Regensburg 2013 – scientific programme

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BP: Fachverband Biologische Physik

BP 2: Proteins

BP 2.1: Topical Talk

Monday, March 11, 2013, 09:30–10:00, H44

Energy conversion mechanisms of heat shock proteins — •Thorsten Hugel — Physik Department and IMETUM, Technische Universität München, Boltzmannstr.11, 85748 Garching, Germany

Single molecule methods allow real time observation of molecular machines at work. We have utilized single molecule Förster Resonance Energy Transfer (smFRET) to decipher the mechano-chemical cycle of the heat shock proteins yeast Hsp90 [1] and bacterial Hsp90 [2]. Although they are homolog we observe significant differences in domain movement and in their mechanism of energy conversion.

To further elucidate the structure-function relationship in these Hsp90s we use optical tweezers and a smFRET based nanopositioning system. Our in vitro results are mostly consistent with the crystal structure of yeast Hsp90 [3], but show some significant deviations in the N-terminal domain.

Finally, these methods are not only suited to determine the structure and function of isolated single proteins, but yield valuable insights into their interplay with other proteins.

[1] Ratzke et al., PNAS (2012) [2] Ratzke et al., JMB (2012) [3] Ali et al., Nature (2006)