Biophysics Journal Club

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins

Wednesday, 14 June 2017 12:00PM PDT
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Biophysics Journal Club
 
Mike Kirkness
SFU Physics
 
Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins
 
Jun 14, 2017 at 12PM
 

Synopsis

Hao Yu, Matthew G. W. Siewny, Devin T. Edwards, Aric W. Sanders, Thomas T. Perkins
Science 355, 945-950 – Published 3 March 2017


Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. Using force spectroscopy optimized for 1-microsecond resolution, we reexamined the unfolding of individual bacteriorhodopsin molecules in native lipid bilayers. The experimental data reveal the unfolding pathway in unprecedented detail. Numerous newly detected intermediates—many separated by as few as two or three amino acids—exhibited complex dynamics, including frequent refolding and state occupancies of <10 ms. Equilibrium measurements between such states enabled the folding free-energy landscape to be deduced. These results sharpen the picture of the mechanical unfolding of membrane proteins and, more broadly, enable experimental access to previously obscured protein dynamics.