Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.

ABSTRACT: Binding of ligands is often crucial for function yet the effects of ligand binding on the mechanical stability and energy landscape of proteins are incompletely understood. Here, we use a combination of single-molecule optical tweezers and MD simulations to investigate the effect of ligand binding on the energy landscape of acyl-coenzyme A (CoA)-binding protein (ACBP). ACBP is a topologically simple and highly conserved four-α-helix bundle protein that acts as an intracellular transporter and buffer for fatty-acyl-CoA and is active in membrane assembly. We have previously described the behavior of ACBP under tension, revealing a highly extended transition state (TS) located almost halfway between the unfolded and native states. Here, we performed force-ramp and force-jump experiments, in c

SUBMITTER: Sonar P 

PROVIDER: S-EPMC7677128 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature