THERMODYNAMICALLY UNSTABLE PROTEINS:
CHANCE OR NECESSITY?


A Wokshop jointly sponsored by Sincrotrone Trieste and the International Center for Theoretical Physics


Adriatico Guesthouse, Grignano (Trieste)
December 14-16, 2009



The aim of the workshop is to discuss why several functionally important mesophile proteins have an intrinsic low thermodynamic stability. Much has been said about proteins, which are intrinsically unfolded since only relatively recently it has been accepted by most that not all proteins, but rather a large portion of them, do not have an intrinsic fold. These unstructured proteins gain a structure only upon interaction with their partners or as a consequence of variations of the environmental conditions. Yet intrinsically unfolded proteins play an essential role in nature.

We would like to put emphasis on a quite different aspect of this concept: several mesophile proteins, also fully structured, may have a limited range of thermodynamic stability. What is this due to? Is this necessary for their function or is it a mere chance of evolution? There are certainly examples in which the protein instability seems to be instrumental for function activation under specific conditions. In other instances, an intrinsic instability could be due only to an evolutionary cul-de-sac, as it seems the case when only one orthologue of a large family is unstable.

This subject is timely also in the view of the current technical possibilities. An important element for considering Trieste as the most suitable venue for this workshop is the necessity of bringing together experimentalists and theoreticians who could tackle the problem in a complementary and synergistic fashion. Trieste has in fact a long tradition in theoretical physics studies. At the same time the presence of the Elettra synchrotron facility at Elettra provides a number of experimental groups with biophysical techniques for the structural characterization of biological molecules.

We hope that the workshop will bring together diverse local expertise and will reinforce fruitful scientific interactions between the two communities. We envisage between 80 to 100 participants, speakers included.

For information please contact: useroffice@elettra.trieste.it


PRELIMINARY PROGRAM

Opening Session I - Thermodynamics
  • George Rose (Bethesda) confirmed
  • Ernesto Freire (Baltimore) confirmed
  • Felix Franks (London) confirmed
  • Gert Vriend (Nijmegen) confirmed
Session II - Disordered and Unstructured Proteins
  • Dimitri Svergun (Hamburg) confirmed
  • Peter Tompa (Budapest) confirmed
  • Pierre Goloubinoff (Lausanne) confirmed
  • Marek Cieplak (Warsaw) confirmed
Session III - Folding
  • Rainher Rudolph (Halle) confirmed
  • Arthur Lesk (Pennsylvania) confirmed
  • Bruno Samori' (Bologna) confirmed
  • Brian Sykes (Alberta) confirmed
Session IV - Cold Denaturation
  • Giuseppe Graziano (Napoli) confirmed
  • Iain Campbell (Oxford) to be confirmed
  • Giancarlo Franzese (Barcelona) confirmed
  • Thomas Szyperski (Buffalo) confirmed
Closing lecture:
  • Piotr Privaloff (Baltimore) confirmed