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. 1974 Jun;1(6):753–759. doi: 10.1093/nar/1.6.753

`DNA snapback' peptides

Robert L Novak 1, James Dohnal 1
PMCID: PMC343377  PMID: 10793754

Abstract

Thermal denaturation studies show that 10-15% of the calf thymus DNA in the heat denatured (Tyr-Gly-Tyr-Gly-Tyr)-DNA complex renatures spontaneously after colling. The double-strandness of this DNA was verified by its resistance to single-strand Neurospora endonuclease and by its elution profile on hydroxypatite columns. The renatured DNA isolated by the latter technique was found to contain 56% GC compared to the 41% GC content of the whole thymus DNA. Alternating tryptophanyl-glycyl and histidyl-glycyl peptides also catalyze the same renaturation. A linear correlation was found between the thermal stabilization afforded to the DNA by the various peptides and their ability to “catalyze” DNA strand renaturation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Novak R. L., Dohnal J. Tyrosyl peptide models for acidic protein-DNA interactions. Nat New Biol. 1973 May 30;243(126):155–157. doi: 10.1038/newbio243155a0. [DOI] [PubMed] [Google Scholar]

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