Probing the non-covalent forces key to the thermodynamics of β-hairpin unfolding.

ABSTRACT: Although it is well understood that the graph of the free energy of unfolding (ΔG) of a globular protein with temperature approximates to a negative parabola, there is as yet no link between this global (G) ΔG _G(T) function and the individual structural elements-residue type and the non-covalent forces between groups-contributing to it. As such, there is little understanding of how each structural element contributes to the globally assessed changes of enthalpy (ΔH _G), entropy (ΔS _G), and heat capacity (ΔC _p(G)) of unfolding calculated from the ΔG _G(T) function. To address this situation, we consider here an alternative approach to examining fold stability. Specifically, we examin

SUBMITTER: Tran TH 

PROVIDER: S-EPMC11369966 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature