Dynamic regulation on energy landscape evolution of single-molecule protein by conformational fluctuation

2012 ◽  
Vol 86 (2) ◽  
Author(s):  
Chien Y. Lin ◽  
Jung Y. Huang ◽  
Leu-Wei Lo
Keyword(s):  
Single Molecule ◽  
Landscape Evolution ◽  
Energy Landscape ◽  
Dynamic Regulation ◽  
Conformational Fluctuation

scholarly journals Slow domain reconfiguration causes power-law kinetics in a two-state enzyme

2018 ◽  
Vol 115 (3) ◽  
pp. 513-518 ◽  
Author(s):  
Iris Grossman-Haham ◽  
Gabriel Rosenblum ◽  
Trishool Namani ◽  
Hagen Hofmann
Keyword(s):  
Free Energy ◽  
Single Molecule ◽  
Power Law ◽  
Energy Landscape ◽  
Rate Equations ◽  
Free Energy Landscape ◽  
Closed Domain ◽  
Single Molecule Fret ◽  
Power Law Kinetics ◽  
Interdomain Interactions

Protein dynamics are typically captured well by rate equations that predict exponential decays for two-state reactions. Here, we describe a remarkable exception. The electron-transfer enzyme quiescin sulfhydryl oxidase (QSOX), a natural fusion of two functionally distinct domains, switches between open- and closed-domain arrangements with apparent power-law kinetics. Using single-molecule FRET experiments on time scales from nanoseconds to milliseconds, we show that the unusual open-close kinetics results from slow sampling of an ensemble of disordered domain orientations. While substrate accelerates the kinetics, thus suggesting a substrate-induced switch to an alternative free energy landscape of the enzyme, the power-law behavior is also preserved upon electron load. Our results show that the slow sampling of open conformers is caused by a variety of interdomain interactions that imply a rugged free energy landscape, thus providing a generic mechanism for dynamic disorder in multidomain enzymes.

Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin

2006 ◽  
Vol 2 (4) ◽  
pp. 282-286 ◽  
Author(s):  
Jasna Brujić ◽  
Rodolfo I. Hermans Z. ◽  
Kirstin A. Walther ◽  
Julio M. Fernandez
Keyword(s):  
Single Molecule ◽  
Energy Landscape ◽  
Force Spectroscopy ◽  
Glassy Dynamics ◽  
Single Molecule Force Spectroscopy

scholarly journals pH-Dependent Deformations of the Energy Landscape of Avidin-like Proteins Investigated by Single Molecule Force Spectroscopy

Molecules ◽  
2014 ◽  
Vol 19 (8) ◽  
pp. 12531-12546 ◽  
Author(s):  
Melanie Köhler ◽  
Andreas Karner ◽  
Michael Leitner ◽  
Vesa Hytönen ◽  
Markku Kulomaa ◽  
...  
Keyword(s):  
Single Molecule ◽  
Energy Landscape ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy ◽  
Ph Dependent
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