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Cited by 1,401

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Coupling of Local Folding to Site-Specific Binding of Proteins to DNA

Spolar, Ruth S., Record, M. Thomas·1994·Science

Abstract

Thermodynamic studies have demonstrated the central importance of a large negative heat capacity change (Δ C ° assoc ) in site-specific protein-DNA recognition. Dissection of the large negative Δ C ° assoc and the entropy change of protein-ligand and protein-DNA complexation provide a thermodynamic signature identifying processes in which local folding is coupled to binding. Estimates of the number of residues that fold on binding obtained from this analysis agree with structural data. Structural comparisons indicate that these local folding transitions create key parts of the protein-DNA interface. The energetic implications of this "induced fit" model for DNA site recognition are considered.

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Metadata

Authors
Spolar, R. S., & Record, M. T.
Venue
Science
Published
1994-02-11
Volume
263
Issue
5148
Pages
777-784
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1965127482
Cited by
1,401
References
1
FWCI
24.27
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Coupling of Local Folding to Site-Specific Binding of Proteins to DNA. https://app.cochat.ai/papers/10.1126/science.8303294
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Spolar, R. S., & Record, M. T. (1994). Coupling of Local Folding to Site-Specific Binding of Proteins to DNA. Science. https://doi.org/10.1126/science.8303294

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.