Preface
Proteins are the major functional molecules of life. They have evolved through selection pressure to perform specific functions. The functional properties of proteins depend upon their three-dimensional structures. One of the great unsolved problems of science is the prediction of the three-dimensional structure of a protein from its amino acid sequence.
The CXLV Course of the International School of Physics “Enrico Fermi” brought together scientists from a variety of areas of protein science and of physics. It provided a unique oportunity for discussions across the borders, at a time in which physicists addicted to simplifications are beginning to learn how much small details can matter in describing the properties of proteins, and molecular biologists are starting to appreciate the usefulness of having numbers attached to arrows of their cartoons and equations relating the numbers.
During the School the subject of protein folding and of protein design and evolution were discussed, both experimentally (W. Eaton, D. Eisenberg, A. Fersht, L. Serrano, V. Goldanskii and M. Oliveberg) and theoretically (R. A. Broglia, A. Finkelstein, A. Maritan, L. Mirny, H. Orland E. Shakhnovich, G. Tiana), as well as their connection to the general subject of polymers and of spin glasses (A. Grosberg, A. Khokhlov, G. Parisi). The audience made out of an extremely gifted group of young students and practitioners, contributed in a very active fashion to the School not only through questions and discussions, but also through the presentation of short, highly articulated seminars, touching on subjects lying at the forefront of protein research.
The lectures started with a review of the field and a discussion of the latest experimental progress in the subject of protein engineering and of protein design by Alan Fersht and Luis Serrano, respectively. Their lectures were central to the School, but are the only ones missing from the Proceedings. If one should look for a reason for this fact, one is reminded that Alan, at the time of the conference, had just published the third edition of his authorative monography Structure and Mechanism in Protein Science (W. H. Freeman Co., New York), while Luis was helping at creating a start-up biomedical venture. It is not easy to write a synthesis of a masterpiece, nor to have much time left over for relaxed writing when one goes private. While these facts did not make any easier the life of the editors of the present Proceedings, they reflect the vitality and breadth of interests the subject of protein folding and design has awaken in the scientific comunity.
On behalf of all the participants to the course we would like to express our gratitude to the Italian Physical Society for providing hospitality in the exquisite setting of Villa Monastero. We want also to thank several funding agencies (NATO, European Union, Unesco) for providing the funds needed to make the whole project a reality.
In the organization of the course it has been a great pleasure to work with Prof. F. Bassani, President of the Italian Physical Society. We would also like to express our thanks to Dr. G. Tiana, who acted as Scientific Secretary of the course, and to pay tribute to the kindness and efficiency of the secretarial staff headed by C. Vasini and B. Alzani.
R. A. Broglia and E. I. Shakhnovich