Protein Engineering Research Institute

Research subjects of the Protein Engineering Research Institute are ... 

Establishing international basic research projects, such as the Protein Engineering Research Institute. 

Department of Protein Engineering, Cancer Institute, Japanese Foundation for Cancer Research and CREST/JST, Toshima,... 

Laboratory of Molecular Biology and Centre for Protein Engineering, Medical Research Council, Camliridge, UK. Present address Institute of Chemical Sciences and Engineering, Ecole Polytechnique F6derale de Lausanne, Lausanne, Switzerland. Correspondence should be addressed to C.H. (Christian.heinis epfl.ch) or G.W. (winter mrc-lmb.cam.ac.uk). 

Danilo Corradini is research director at the Institute of Chemical Methodologies of the Italian National Research Council (CNR) and a member of the General Scientific Advisory Board of CNR. His involvement in separation science started in 1976 with his research work on chromatography and electrophoresis for his PhD studies in chemistry, which was carried out at Sapienza University of Rome, Italy, under the direction of Michael Lederer, founder and first editor of the Journal of Chromatography. In 1983-1984, he worked with Csaba Horvath, the pioneer of HPLC, at the Department of Chemical Engineering at Yale University, New Haven, Connecticut, where he initiated his first investigations on the HPLC of proteins and peptides, which he continued at the Institute of Chromatography of CNR after he returned to Italy. 

For many years, die nature and location of the complex of proteins (sometimes referred to as the engine of photosynthesis) were poorly understood. During the 1980s, much more was learned as the result of research carried out by Johann Deisenhofer (Howard Hughes Medical Institute), Robert Huber, and Harmut Michel (Max Planck Institute), and for this work the investigators were awarded the 1988 Nobel Prize for chemistry. The protein complex, called the membrane-bound proteins, are difficult to define structurally because they do not crystallize readily and thus could not be subjected to x-ray crystallography. However, over a period of three years, the researchers were able to create crystals and thus were able to determine precisely the position of some 10,000 atoms in the protein complex. 

Michael E. Paulaitis is Professor of Chemical and Biomolecular Engineering and Ohio Eminent Scholar at Ohio State University. He is also Director of the Institute of Multiscale Modeling of Biological Interactions at Johns Hopkins University. His research focuses on molecular thermodynamics of hydration, protein solution thermodynamics, and molecular simulations of biological macromolecules. 

Massachusetts Institute of Technology and his Ph.D. in chemical engineering at Princeton University. While at Princeton, his research was directed by Arthur V. Tobolsky in the area of polymer physical chemistry. He is currently professor of chemical engineering at the University of Wisconsin where, since 1967, he has been active in polymer research. He has published more than 80 papers on topics covering polyurethane block polymers, inomers, polymer yield mechanisms, composites, and fiber physics. His current research includes studies of protein and thrombus deposition on polymers used in biomedical applications. Professor Cooper is a Fellow of the American Physical Society and has served on the Board of Trustees of Argonne Universities Association. 

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