Membrane-Protein Unfolding Intermediates Detected with Enhanced Precision Using a Zigzag Force Ramp.

ABSTRACT: Precise quantification of the energetics and interactions that stabilize membrane proteins in a lipid bilayer is a long-sought goal. Toward this end, atomic force microscopy has been used to unfold individual membrane proteins embedded in their native lipid bilayer, typically by retracting the cantilever at a constant velocity. Recently, unfolding intermediates separated by as few as two amino acids were detected using focused-ion-beam-modified ultrashort cantilevers. However, unambiguously discriminating between such closely spaced states remains challenging, in part because any individual unfolding trajectory only occupies a subset of the total number of intermediates. Moreover, structural assignment of these intermediates via worm-like-chain analysis is hindered by brief dwell times com

SUBMITTER: Jacobson DR 

PROVIDER: S-EPMC7002910 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature