Intrinsic rates and activation free energies from single-molecule pulling experiments.
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.
Dudko
Olga K
OK
Mathematical and Statistical Computing Laboratory, Division of Computational Bioscience, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892, USA.
Hummer
Gerhard
G
Szabo
Attila
A
D001703:Biophysics / Q000379:methods*; D003198:Computer Simulation; D064211:Connectin; D003627:Data Interpretation, Statistical; D007700:Kinetics; D008846:Micromanipulation; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D009124:Muscle Proteins / Q000737:chemistry; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry; D012313:RNA / Q000737:chemistry; D013314:Stress, Mechanical; D013816:Thermodynamics; D013997:Time Factors
D064211:Connectin; D009124:Muscle Proteins; D012313:RNA; D011494:Protein Kinases