title: Direct measurement of protein energy landscape roughness.
abstract: 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 epsilon for a complex consisting of the small GTPase Ran and the nuclear transport receptor importin-beta. The results gave epsilon > 5k(B)T, indicating a bumpy energy surface, which is consistent with the ability of importin-beta to accommodate multiple conformations and to interact with different, structurally distinct ligands.
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Reinat
authors.initials: R
authors.lastname: Nevo
authors.forename: Vlad
authors.initials: V
authors.lastname: Brumfeld
authors.forename: Ruti
authors.initials: R
authors.lastname: Kapon
authors.forename: Peter
authors.initials: P
authors.lastname: Hinterdorfer
authors.forename: Ziv
authors.initials: Z
authors.lastname: Reich
mesh_terms: D008958:Models, Molecular; D011485:Protein Binding; D017510:Protein Folding; D013057:Spectrum Analysis; D013816:Thermodynamics; D028961:beta Karyopherins / Q000737:chemistry*; D020931:ran GTP-Binding Protein / Q000737:chemistry*
chemical_list: D028961:beta Karyopherins; D020931:ran GTP-Binding Protein