2007/05/22 by Alberto Imparato, Stefano Luccioli, Alessandro Torcini
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Advanced Thermodynamics and Statistical Mechanics #Chemistry #Energy landscape #Folding (DSP implementation) #Force Microscopy Techniques and Applications #Function (biology) #Lattice (music) #Materials science #Physical chemistry #Physics #Protein Structure and Dynamics #Protein folding #Range (aeronautics) #Reaction coordinate #Statistical physics #Thermodynamics #cond-mat.stat-mech #q-bio.BM
paper · pdf · doi:10.1103/physrevlett.99.168101
published as Phys. Rev. Lett. 99, 168101 (2007)
arxiv created 2007/05/22 · openalex publication_date 2007/10/15 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
The equilibrium free-energy landscape of an off-lattice model protein as a function of an internal (reaction) coordinate is reconstructed from out-of-equilibrium mechanical unfolding manipulations. This task is accomplished via two independent methods: by employing an extended version of the Jarzynski equality (EJE) and the protein inherent structures (ISs). In a range of temperatures around the "folding transition" we find a good quantitative agreement between the free energies obtained via EJE and IS approaches. This indicates that the two methodologies are consistent and able to reproduce equilibrium properties of the examined system. Moreover, for the studied model the structural transitions induced by pulling can be related to thermodynamical aspects of folding.