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Early Proteins

  • Chapter
The Chemistry of Life’s Origins

Part of the book series: NATO ASI Series ((ASIC,volume 416))

Summary

The nature and function of contemporary proteins are described. Different attempts to synthesize peptides from their component amino acids under conditions that ressemble those of the primitive Earth have been made. Experimental evidence is given for selective condensation of amino acids in water via the intermediary formation of N-carboxyanhydride. Selective resistance toward degradation of β-pleated sheet conformation exemplifies a possible accumu lation of homochiral sequences made of hydrophilic and strong hydrophobic residues. Peptides containing basic amino acids strongly accelerate the hydrolysis of oligoribonucleotides. The peptides bind to the oligonucleotides and undergo a coil to β-sheet transition which plays a determinant role in the observed chemical activity.

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Authors and Affiliations

  1. Centre de Biophysique Moléculaire, 1A, Avenue de la Recherche Scientifique, 45071, Orléans Cedex 2, France

    A. Brack

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  1. A. Brack
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Editors and Affiliations

  1. Laboratory Astrophysics, University of Leiden, Leiden, The Netherlands

    J. M. Greenberg  & C. X. Mendoza-Gómez  & 

  2. Istituto di Fisica, Università di Catania, Catania, Italy

    V. Pirronello

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© 1993 Springer Science+Business Media Dordrecht

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Brack, A. (1993). Early Proteins. In: Greenberg, J.M., Mendoza-Gómez, C.X., Pirronello, V. (eds) The Chemistry of Life’s Origins. NATO ASI Series, vol 416. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-1936-8_14

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  • DOI: https://doi.org/10.1007/978-94-011-1936-8_14

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-4856-9

  • Online ISBN: 978-94-011-1936-8

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