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The Genetic Algorithm and Protein Tertiary Structure Prediction

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Abstract

In 1959, Anfinsen demonstrated that the primary structure (the sequence of amino acids) of a protein can uniquely determine its tertiary structure (three dimensional conformation). This implied that there must be a consistent set of rules for deriving a protein’s tertiary structure from its primary structure. The search for these rules is known as the protein folding problem. Despite many creative attempts, these rules have not been determined (Fasman, 1989). Currently, the primary structures of approximately 40,000 proteins are known. However, only a small percentage of those proteins have known, tertiary structures. A solution to the protein folding problem will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analysis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein folding process. The search for these rules is therefore an important objective for theoretical molecular biology.

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© 1994 Birkhäuser Boston

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Le Grand, S.M., Merz, K.M. (1994). The Genetic Algorithm and Protein Tertiary Structure Prediction. In: Merz, K.M., Le Grand, S.M. (eds) The Protein Folding Problem and Tertiary Structure Prediction. Birkhäuser Boston. https://doi.org/10.1007/978-1-4684-6831-1_4

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  • DOI: https://doi.org/10.1007/978-1-4684-6831-1_4

  • Publisher Name: Birkhäuser Boston

  • Print ISBN: 978-1-4684-6833-5

  • Online ISBN: 978-1-4684-6831-1

  • eBook Packages: Springer Book Archive

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