Mechanistic Insight into the Mechanical Unfolding of the Integral Membrane Diacylglycerol Kinase.

ABSTRACT: The essential forces stabilizing membrane proteins and governing their folding and unfolding are difficult to decipher. Single-molecule atomic force spectroscopy mechanically unfolds individual membrane proteins and quantifies their dynamics and energetics. However, it remains challenging to structurally assign unfolding intermediates precisely and to deduce dominant interactions between specific residues that facilitate either the localized stabilization of these intermediates or the global assembly of membrane proteins. Here, we performed force spectroscopy experiments and multiscale molecular dynamics simulations to study the unfolding pathway of diacylglycerol kinase (DGK), a small trimeric multispan transmembrane enzyme. The remarkable agreement between experiments and simulations all

SUBMITTER: Yang H 

PROVIDER: S-EPMC11040704 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature