On the Interpretation of Force-Induced Unfolding Studies of Membrane Proteins Using Fast Simulations.

ABSTRACT: Single-molecule force spectroscopy has proven extremely beneficial in elucidating folding pathways for membrane proteins. Here, we simulate these measurements, conducting hundreds of unfolding trajectories using our fast Upside algorithm for slow enough speeds to reproduce key experimental features that may be missed using all-atom methods. The speed also enables us to determine the logarithmic dependence of pulling velocities on the rupture levels to better compare to experimental values. For simulations of atomic force microscope measurements in which force is applied vertically to the C-terminus of bacteriorhodopsin, we reproduce the major experimental features including even the back-and-forth unfolding of single helical turns. When pulling laterally on GlpG to mimic the experiment, we

SUBMITTER: Wang Z 

PROVIDER: S-EPMC6817726 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature