Direct measurement of protein energy landscape roughness

被引：79

作者：

Nevo, R

Brumfeld, V

Kapon, R

Hinterdorfer, P

Reich, Z ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel

[2] Weizmann Inst Sci, Dept Plant Sci, IL-76100 Rehovot, Israel

[3] Univ Linz, Inst Biophys, A-4040 Linz, Austria

来源：

EMBO REPORTS | 2005年 / 6卷 / 05期

关键词：

energy landscapes; protein folding and binding; roughness; single-molecule experiments; dynamic force spectroscopy;

D O I：

10.1038/sj.embor.7400403

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：482 / 486

页数：5

共 38 条

[11] Structure of importin-β bound to tbe IBB domain of importin-α [J].