Resumen: Single-molecule force spectroscopy is a powerful technique based on the application of controlled forces to macromolecules. In order to relate the measured response of the molecule to its equilibrium and dynamic properties, a suitable physical picture of the involved process is necessary. In this work, we introduce a plausible model for mechanical unbinding of some molecular complexes, based on a novel free energy profile. We combine two standard theoretical frameworks for analyzing force spectroscopy experiments on two protein:protein complexes, obtaining key magnitudes of the underlying free energy profile, which are only understood within the mentioned model. Additionally, we carry out detailed stochastic dynamics simulations to prove the validity of the analysis protocol and the reliability of the free energy profile. Remarkably, we can compare directly the obtained unbinding free energies with the previously known bulk binding free energies, bridging the gap between bulk and single molecule techniques. Idioma: Inglés DOI: 10.1039/c6cp07508h Año: 2017 Publicado en: PHYSICAL CHEMISTRY CHEMICAL PHYSICS 19, 6 (2017), 4567-4575 ISSN: 1463-9076 Factor impacto JCR: 3.906 (2017) Categ. JCR: PHYSICS, ATOMIC, MOLECULAR & CHEMICAL rank: 9 / 36 = 0.25 (2017) - Q1 - T1 Categ. JCR: CHEMISTRY, PHYSICAL rank: 46 / 146 = 0.315 (2017) - Q2 - T1 Factor impacto SCIMAGO: 1.686 - Physics and Astronomy (miscellaneous) (Q1) - Physical and Theoretical Chemistry (Q1)