Curvature and Torsion of Protein Main Chain as Local Order Parameters of Protein Unfolding.

ABSTRACT: Thermal protein unfolding resembles a global (two-state) phase transition. At the local scale, protein unfolding is, however, heterogeneous and probe dependent. Here, we consider local order parameters defined by the local curvature and torsion of the protein main chain. Because chemical shifts (CS's) measured by NMR spectroscopy are extremely sensitive to the local atomic environment, CS has served as a local probe of thermal unfolding of proteins by varying the position of the atomic isotope along the amino acid sequence. The variation of the CS of each C^α atom along the sequence as a function of the temperature defines a local heat-induced denaturation curve. We demonstrate that these local heat-induced denaturation curves mirror the local protein nativeness defined by the fr

SUBMITTER: Grassein P 

PROVIDER: S-EPMC7362589 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature