Intrinsic Rates and Activation Free Energies From Single-Molecule Pulling Experiments

Phys Rev Lett. 2006 Mar 17;96(10):108101. doi: 10.1103/PhysRevLett.96.108101. Epub 2006 Mar 15.

Abstract

We present a unified framework for extracting kinetic information from single-molecule pulling experiments at constant force or constant pulling speed. Our procedure provides estimates of not only (i) the intrinsic rate coefficient and (ii) the location of the transition state but also (iii) the free energy of activation. By analyzing simulated data, we show that the resulting rates of force-induced rupture are significantly more reliable than those obtained by the widely used approach based on Bell's formula. We consider the uniqueness of the extracted kinetic information and suggest guidelines to avoid over-interpretation of experiments.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Biophysics / methods*
  • Computer Simulation
  • Connectin
  • Data Interpretation, Statistical
  • Kinetics
  • Micromanipulation
  • Models, Chemical
  • Models, Molecular
  • Molecular Conformation
  • Muscle Proteins / chemistry
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Denaturation
  • Protein Folding
  • Protein Kinases / chemistry
  • RNA / chemistry
  • Stress, Mechanical
  • Thermodynamics*
  • Time Factors

Substances

  • Connectin
  • Muscle Proteins
  • RNA
  • Protein Kinases