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Protein-Nucleic Acid Interactions Models and Reality

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Specificity in Biological Interactions
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Abstract

The simple schemes which can be drawn on a theoretical basis for protein- nucleic acid interactions are only rarely observed in reality. Complexes between individual amino acids and nucleotides or their constituents are hard to crystallize and even then, interactions are often not as expected. If nucleotides or single stranded polynucleotides bind to proteins, they unfold with torsion angle γ(O5,-C5,-C4,-C3,) in -sc or ap range instead of the usually preferred +sc. In this form, phosphate-sugar-base can interact better with protein active sites. On the other hand, double stranded DNA maintains its helical structure and proteins associate by inserting α-helices in major grooves as suggested by model building studies with repressor molecules.

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© 1984 Pontificia Academia Scientiarum — Città del Vaticano

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Saenger, W. (1984). Protein-Nucleic Acid Interactions Models and Reality. In: Chagas, C., Pullman, B. (eds) Specificity in Biological Interactions. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-6457-0_6

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  • DOI: https://doi.org/10.1007/978-94-009-6457-0_6

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-009-6459-4

  • Online ISBN: 978-94-009-6457-0

  • eBook Packages: Springer Book Archive

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