Protein Structure and Protein Engineering

1. Front Matter

   Pages I-XI

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2. How Does ATP Make Work?

   • W. P. Jencks

   Pages 1-5

3. Hydrophobic Interactions in Proteins

   • P. L. Privalov

   Pages 6-15

4. Is There a Code for Protein Folding?

   • R. Jaenicke

   Pages 16-36

5. The Method of Protein Structure Determination by NMR in Solution: Initial New Insights Relating to Molecular Mobility

   • K. Wüthrich

   Pages 37-44

6. A Calculated Conformation for the Folding Transition State of Bovine Pancreatic Trypsin Inhibitor

   • M. Levitt

   Pages 45-50

7. Conformational Entropy and Protein Stability

   • K. A. Dill, D. O. V. Alonso

   Pages 51-58

8. The Improvement of Catalytic Effectiveness of an Enzyme: Pseudorevertant Triosephosphate Isomerases Obtained by Random Mutagenesis of Catalytically Sluggish Mutants

   • S. C. Blacklow, J. D. Hermes, J. R. Knowles

   Pages 59-64

9. Reaction Coordinate Approach to the Binding of Ligands to Carboxypeptidase A

   • D. W. Christianson, W. N. Lipscomb

   Pages 65-74

10. The Specific Interaction of Human Leukocyte Elastase with Various Protein Inhibitors

    • W. Bode

    Pages 75-85

11. The Interplay Between Enzyme Mechanism, Protein Structure, and Inhibitor and Catalyst Design

    • P. A. Bartlett

    Pages 86-95

12. Evolution of Hemoglobin as Studied by Protein Engineering and X-Ray Crystallography

    • D. Altschuh, J. Tame, K. Nagai

    Pages 96-108

13. Design and Construction of Biologically Active Peptides and Proteins Including Enzymes

    • E. T. Kaiser

    Pages 109-112

14. Computer Modeling with a Protein Data Base

    • T. A. Jones

    Pages 113-115

15. Automated and High-Speed DNA Sequencing - Computer Technology Promotes Biological Advances

    • A. Wada

    Pages 116-122

16. Synthetic Antibodies with a Known Three-Dimensional Structure

    • A. Plückthun, A. Skerra, R. Glockshuber, J. Stadlmüller

    Pages 123-131

Protein engineering has had considerable impact on basic and applied research in biochemistry and molecular biology. It is already in use as a tool in molecular biology, but it is beginning to strongly influence the planning of experiments in biology everywhere, and, with even fur­ ther-reaching consequences, the appointment politics in research in­ stitutions and industries. Protein engineering, perhaps more than any other methods of protein analysis and peptide synthesis, has shown that proteins are organic molecules governed by the universal laws of chemistry and physics. How­ ever, as was the case with other new powerful methods and techniques, protein engineering tempts to an exploration of its limitations and thus generates more questions than it answers. The 39th Mosbacher Colloquium on Protein Structure and Protein Engi­ neering is not the first conference on this topic and it will not be the last. The important issues are obviously techniques of protein en­ gineering, examples of application, and the basic framework of protein structure and stability within which reasonable experiments can be de­ signed; conversely also, what we can learn about protein structure, dynamics, and folding from such experiments. Experiments in this direc­ tion aim at elucidating the folding code in the long run, but help to exploit the role of individual amino acid residues in catalysis, pro­ tein stability, and binding specificity in selected proteins now.

• ATP
• DNA
• DNA sequencing
• base
• enzymes
• mutagenesis
• protein
• reaction

• Labor für Molekularbiologie, Genzentrum, Martinsried, Germany

  Ernst-Ludwig Winnacker

• Max-Planck-Institut für Biochemie, Martinsried, Germany

  Robert Huber

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