Unusually Strong Positive Cooperativity in Binding of Peptides to Latent Membrane Protein‐1 DNA Fragments of the Epstein–Barr Viral Gene

@article{Yang2006UnusuallySP,
  title={Unusually Strong Positive Cooperativity in Binding of Peptides to Latent Membrane Protein‐1 DNA Fragments of the Epstein–Barr Viral Gene},
  author={Chia-Hung Yang and Kee Ching G. Jeng and Wan-Hsu Yang and Yu-ling Chen and Chia-Chun Hung and Juey-Wen Lin and Shui-Tein Chen and Simon Richardson and Christopher R. H. Martin and Michael J. Waring and Leung Sheh},
  journal={ChemBioChem},
  year={2006},
  volume={7}
}
The DNA‐binding preferences of two oligopeptide amides, (His‐Pro‐Arg‐Lys)3NH2 (HR‐12) and (Ser‐Pro‐Arg‐Lys)3NH2 (SP‐12), have been examined by quantitative DNase I footprinting studies. Two different DNA fragments were investigated: a pair of 5′‐32P‐labeled duplexes from pBR322 with one or other of the complementary strands labeled and a corresponding pair of 5′‐32P‐labeled duplexes representing fragments of the latent membrane protein (LMP‐1) gene from a pathogenic Epstein–Barr virus variant… 
Determination of Allosteric Effects and Interstrand Bidentate Interactions in DNA‐Peptide Molecular Recognition
TLDR
The interconnection of DNA footprints of peptides HypKK-10 and the parent peptide PyPro-12 supports the proposal that interaction network cooperativity is preferred in DNA-peptide interactions between multiple recognition sites.
Novel DNA-peptide interaction networks.
Investigation of various fluorescent protein–DNA binding peptides for effectively visualizing large DNA molecules
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This investigation provided HMG-tagged FP–DBP as the best DNA staining reagent in terms of fluorescence intensity, signal-to-noise ratio, and DNA binding affinity (Kd = 586 nM).
Enthalpy-driven nuclease-like activity and mechanism of peptide-chlorambucil conjugates.
TLDR
The strongly enthalpy-driven binding of CLB-peptide conjugates to preferred loci in DNA furnishes the required proximity effect to generate the observed nuclease-like sequence-selective cleavage.
Energetic studies on DNA-peptide interaction in relation to the enthalpy-entropy compensation paradox.
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It is concluded that the preservation of a rather narrowly-defined ΔG value is central to the EEC in DNA-peptide interactions, illuminating the universal EEC paradox commonly found in diverse biochemical reactions.

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