Coupling of Local Folding to Site-Specific Binding of Proteins to DNA
10.1126/science.8303294
Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
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.

Bibliography

Spolar, R. S., & Record, M. T. (1994). Coupling of Local Folding to Site-Specific Binding of Proteins to DNA. Science, 263(5148), 777–784.

Authors 2
  1. Ruth S. Spolar (first)
  2. M. Thomas Record (additional)
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Dates
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Created 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.)
Deposited 1 year, 7 months ago (Jan. 15, 2024, 5:37 a.m.)
Indexed 4 hours, 45 minutes ago (Aug. 27, 2025, 12:31 p.m.)
Issued 31 years, 6 months ago (Feb. 11, 1994)
Published 31 years, 6 months ago (Feb. 11, 1994)
Published Print 31 years, 6 months ago (Feb. 11, 1994)
Funders 0

None

@article{Spolar_1994, title={Coupling of Local Folding to Site-Specific Binding of Proteins to DNA}, volume={263}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.8303294}, DOI={10.1126/science.8303294}, number={5148}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Spolar, Ruth S. and Record, M. Thomas}, year={1994}, month=feb, pages={777–784} }