Diverse Folding Pathways of HIV-1 Protease Monomer on a Rugged Energy Landscape.

ABSTRACT: The modern energy landscape theory of protein folding predicts multiple folding pathways connecting a myriad of unfolded conformations and a well-defined folded state. However, direct experimental observation of heterogeneous folding pathways is difficult. Naturally evolved proteins typically exhibit a smooth folding energy landscape for fast and efficient folding by avoiding unfavorable kinetic traps. In this case, rapid fluctuations between unfolded conformations result in apparent two-state behavior and make different pathways indistinguishable. However, the landscape roughness can be different, depending on the selection pressures during evolution. Here, we characterize the unusually rugged folding energy landscape of human immunodeficiency virus-1 protease monomer using single-molecul

SUBMITTER: Yoo J 

PROVIDER: S-EPMC6817636 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature