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The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.

Publication ,  Journal Article
Chilkoti, A; Boland, T; Ratner, BD; Stayton, PS
Published in: Biophysical journal
November 1995

The interaction forces between biotin and a set of streptavidin site-directed mutants with altered biotin-binding equilibrium and activation thermodynamics have been measured by atomic force microscopy. The AFM technique readily discriminates differences in interaction force between the site-directed (Trp to Phe or Ala) mutants. The interaction force is poorly correlated with both the equilibrium free energy of biotin binding and the activation free energy barrier to dissociation of the biotin-streptavidin complex. The interaction force is generally well correlated with the equilibrium biotin-binding enthalpy as well as the enthalpic activation barrier, but in the one mutant where these two parameters are altered in opposite directions, the interaction force is clearly correlated with the activation enthalpy of dissociation. These results suggest that the AFM force measurements directly probe the enthalpic activation barrier to ligand dissociation.

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Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

November 1995

Volume

69

Issue

5

Start / End Page

2125 / 2130

Related Subject Headings

  • Thermodynamics
  • Streptavidin
  • Recombinant Proteins
  • Mutagenesis, Site-Directed
  • Microscopy, Atomic Force
  • Ligands
  • Kinetics
  • Biotin
  • Biophysics
  • Biophysics
 

Citation

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Chilkoti, A., Boland, T., Ratner, B. D., & Stayton, P. S. (1995). The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophysical Journal, 69(5), 2125–2130. https://doi.org/10.1016/s0006-3495(95)80083-4
Chilkoti, A., T. Boland, B. D. Ratner, and P. S. Stayton. “The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.Biophysical Journal 69, no. 5 (November 1995): 2125–30. https://doi.org/10.1016/s0006-3495(95)80083-4.
Chilkoti A, Boland T, Ratner BD, Stayton PS. The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophysical journal. 1995 Nov;69(5):2125–30.
Chilkoti, A., et al. “The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.Biophysical Journal, vol. 69, no. 5, Nov. 1995, pp. 2125–30. Epmc, doi:10.1016/s0006-3495(95)80083-4.
Chilkoti A, Boland T, Ratner BD, Stayton PS. The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophysical journal. 1995 Nov;69(5):2125–2130.
Journal cover image

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

November 1995

Volume

69

Issue

5

Start / End Page

2125 / 2130

Related Subject Headings

  • Thermodynamics
  • Streptavidin
  • Recombinant Proteins
  • Mutagenesis, Site-Directed
  • Microscopy, Atomic Force
  • Ligands
  • Kinetics
  • Biotin
  • Biophysics
  • Biophysics