F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements

Synopsis

Authors: Mitsuhiro Sugawaa, Kei-ichi Okazakib, Masaru Kobayashia, Takashi Matsuia, Gerhard Hummerb, Tomoko Masaikea, and Takayuki Nishizakaa

PNAS 2016 ; published ahead of print May 10, 2016, doi:10.1073/pnas.1524720113

​Research investigating protein structure, function, and dynamics is possibly the only scientific topic of conversation equally relevant to experimentalists, medical professionals, theorists, and programmers alike. Our current models of the function of specific proteins are inferred from the information we do know, and are continuously updated to agree with all (most) past conclusions.

This recent paper tests our understanding of F1-ATPase by simultaneously measuring the structural states of the 3 sub units using FRET and tracking rotational angle. While the conclusions do not overhaul our present understanding of the F1 system, this paper serves as a reminder that just because we have a cartoon model, doesn't mean the story should be taken as complete or correct. As experimental techniques continue to advance, it is important to use our new tools to confirm what has been assumed as true.