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Chemical and biological evolution of a nucleotide-binding protein

Nature volume 250, pages 194–199 (1974)Cite this article

Abstract

Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone would fail. Minimum base changes per codon can then be used to measure evolutionary distances which suggest that this structure was present during precellular evolution.

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Authors and Affiliations

  1. Department of Biological Sciences, Purdue University, West Lafayette, Indiana, 47907

    Michael G. Rossmann, Dino Moras & Kenneth W. Olsen

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  1. Michael G. Rossmann
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  2. Dino Moras
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  3. Kenneth W. Olsen
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Rossmann, M., Moras, D. & Olsen, K. Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194–199 (1974). https://doi.org/10.1038/250194a0

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