Designer proteins in biotechnology

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Abstract
The 86th International Titisee Conference, sponsored by the Boehringer Ingelheim Fonds (http://www.bifonds.de), was organized by Franz Xaver Schmid, University of Bayreuth, Germany, and Reinhard Sterner, University of Cologne, Germany. It was held during 23–27 October 2002, in the town of Titisee in the Black Forest, Germany. ![][1] The structural and functional complexity of proteins as heteropolymeric polypeptide chains is based on diverse interactions between a variety of their hydrophobic, polar and ionizable side chains. These interactions occur in unliganded proteins as well as on association with ligands. This complexity makes it difficult to predict accurately the structure and function of a protein from its primary sequence. Given the vast amount of sequence information produced from the genome projects, as well as the discovery that certain diseases are due to aberrant protein structures such as amyloid fibrils, there is an increasing need for a better understanding of protein structure and function at the molecular level. In recent years, progress in predicting protein structure and in the development of new techniques on the basis of evolutionary concepts has led to the design of proteins with improved properties and new functions. The 86th International Titisee Conference highlighted these emerging possibilities. About 60 scientists, working in both basic and applied protein chemistry, discussed new developments from the use of structure‐based rational design and in vitro evolution strategies. This new research has been developed in many areas, including knowledge‐based structure prediction, protein stability, protein–protein and protein–ligand interactions, enzyme catalysis and protein design. In this report, some of the work that was presented is discussed. The selection reflects the author's interests rather than the quality of the talks, which were all excellent. ### Protein stability The three‐dimensional structure of a protein is stabilized by hydrogen bonding, van der Waal's interactions, and other polar and non‐polar interactions. Although each individual interaction … [1]: pending:yes