Institute of Sciences, Arts and Letters

August 29, 2013 – 01:55

XV SCHOOL OF PURE AND APPLIED BIOPHYSICS

Protein stability and pathways of self-assembly

Institute of Sciences, Arts and Letters
Palazzo Franchetti
Venice, Campo S. Stefano
January 24-28, 2011

SCHOOL AND PROGRAM OVERVIEW
Thermodynamic and conformational stability of proteins in solution is a main issue in many fields: pathological protein deposition in neurodegenerative diseases, industrial separation processes by salt-induced precipitation,
pharmaceutical formulation, protein crystallization, or protein gelation (which is relevant, eg, in the food industry).
In this context, the study of common pathways leading to different biologically relevant structures (crystals, fibrils, amorphous aggregates) has a pivotal importance.
The control and design of a specific morphology require a detailed knowledge of the molecular interactions and the basic mechanisms involved in. aggregation.
The school will address this theme by covering several subjects from the physical chemistry of biomolecular solution to the mechanism of protein self-assembly and the strategies for a rational drug design, protein stability without Affecting Which Enhances protein activity and function.
The school Focuses on contemporary biophysical topics.
The selected subjects will draw Young Researchers' attention to frontier research issues of considerable scientific and educational impact.
The School will be held in the magnificent Palazzo Franchetti, the seat of the Istituto Veneto located in the historical center of Venice.
In 2011, the school is the subject of Protein Stability and Pathways of Self Assembly covering the Following topics:
1. Protein folding and conformational stability
2. Cold denaturation
3. Protein stability in crowded environments
4. Thermodynamics of protein solutions
5. Protein interactions and phase transitions
6. Mechanisms of protein self-assembly
7. Misfolding and aggregation
8. Conformational diseases

Lecturers:
Fabrizio Chiti, University of Florence (Italy)
Ernesto Freire, Johns Hopkins University, Baltimore, MD (USA)
Stefano Gianni, University of Rome "La Sapienza", Rome (Italy)
Richard Goldstein, National Institute for Medical Research, London (UK)
Abraham M. Lenhoff, University of Delaware, Newark, DE (USA)
Davi d A. Lomas, Cambridge Institute for Medical Research, Cambridge (UK)
Vincenzo Martorana, Institute of Biophysics, Palermo (Italy)
Annalisa Pastore, National Institute for Medical Research, London (UK)
Christian Rischel, Protein Structure and Biophysics, Copenhagen (Denmark)
Christopher J. Roberts, University of Delaware, Newark, DE (USA)
Pierandrea Temussi, University of Naples "Federico II" (Italy)
Guido Tiana, University of Milan (Italy)
Bente Vestegaard, Department of Medicinal Chemistry, Copenhagen (Denmark)
Roland Winter, Technische Universität Dortmund (Germany)
Emanuela Zaccarelli, University of Rome "La Sapienza" (Italy)

Source: www.istitutoveneto.it

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