Premium
Direct measurement of protein energy landscape roughness
Author(s) -
Nevo Reinat,
Brumfeld Vlad,
Kapon Ruti,
Hinterdorfer Peter,
Reich Ziv
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400403
Subject(s) - energy landscape , folding (dsp implementation) , importin , force spectroscopy , chemical physics , energy (signal processing) , surface finish , protein folding , spectroscopy , physics , molecule , nuclear transport , biophysics , chemistry , materials science , biology , biochemistry , thermodynamics , cell nucleus , nuclear magnetic resonance , quantum mechanics , mechanical engineering , engineering , composite material , gene
The energy landscape of proteins is thought to have an intricate, corrugated structure. Such roughness should have important consequences on the folding and binding kinetics of proteins, as well as on their equilibrium fluctuations. So far, no direct measurement of protein energy landscape roughness has been made. Here, we combined a recent theory with single‐molecule dynamic force spectroscopy experiments to extract the overall energy scale of roughness ε for a complex consisting of the small GTPase Ran and the nuclear transport receptor importin‐β. The results gave ε >5 k B T , indicating a bumpy energy surface, which is consistent with the ability of importin‐β to accommodate multiple conformations and to interact with different, structurally distinct ligands.