Overview
- Editors:
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Shmuel Cabilly
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Weizmann Institute of Science, Rehovot, Israel
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Table of contents (26 protocols)
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Front Matter
Pages i-xiii
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- Colette T. Dooley, Richard A. Houghten
Pages 13-24
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- Achim Kramer, Jens Schneider-Mergener
Pages 25-39
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- John M. Ostresh, Barbara Dörner, Richard A. Houghten
Pages 41-49
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- Zhou Songyang, Lewis C. Cantley
Pages 87-98
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- Werner J. Tegge, Ronald Frank
Pages 99-106
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- Channa K. Jayawickreme, Shiranthi P. Jayawickreme, Michael R. Lerner
Pages 107-118
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- Channa K. Jayawickreme, Shiranthi P. Jayawickreme, Michael R. Lerner
Pages 119-128
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- Baruch Stern, Jonathan M. Gershoni
Pages 137-154
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- Alessandra Luzzago, Franco Felici
Pages 155-164
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- Shmuel Cabilly, Judith Heldman, Eliahu Heldman, Ephraim Katchalski-Katzir
Pages 175-183
About this book
During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed "inert. " This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu.
Editors and Affiliations
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Weizmann Institute of Science, Rehovot, Israel
Shmuel Cabilly
