Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET.

ABSTRACT: A protein fold is defined as a structural arrangement of a secondary structure in a three-dimensional space. It would be interesting to know whether a particular fold can be assigned to certain features of the corresponding folding/unfolding transitions. To understand the underlying principles of the manifold folding transitions in more detail, single-molecule FRET is the method of choice. Taking the two-domain protein phosphoglycerate kinase (PGK) as an example, we investigated denaturant-induced unfolded states of PGK using the above method. For this purpose, different intramolecular distances within the two domains were measured. In addition to the known two-state transition, a transition with a compact folding intermediate was also identified in each of the two domains. Based on the st

SUBMITTER: Bustorff N 

PROVIDER: S-EPMC10526189 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature