Abstract
The complex between the tumor suppressor p53 and its down-regulator Mdm2 has been studied by dynamic force spectroscopy and the unbinding data have been analyzed in the framework of the Jarzynski theoretical approach. Accordingly, the unbinding equilibrium free energy has been determined from the work done along several non-equilibrium paths from the bound to the unbound state in the single molecule regime. An unbinding free energy of -8.4 kcal mol(-1) has been found for the complex; such a value is in a good agreement with that measured both in the bulk by isothermal titration calorimetry and that obtained from theoretical computing at the single molecule level. The determination of the unbinding free energy, together with the knowledge of the dissociation rate constant and energy barrier width, as previously obtained by dynamic force spectroscopy, adds rewarding insights on the energy landscape for this complex which is currently at the focus of anticancer drug design.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
