The energetics of T4 lysozyme reveal a hierarchy of conformations

被引：0

作者：

Manuel Llinás

Blake Gillespie

Frederick W. Dahlquist

Susan Marqusee

机构：

[1] 229 Stanley Hall,Department of Molecular and Cell Biology

[2] University of California,Institute of Molecular Biology and Departments of Chemistry and Physics

[3] Berkeley,undefined

[4] University of Oregon,undefined

来源：

Nature Structural Biology | 1999年 / 6卷

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摘要：

We have used native state exchange to examine the energy landscape of the well-characterized protein T4 lysozyme. Although the protein exhibits two-state behavior by traditional probes, the energy landscape determined here is much more complex. The average stability of the C-terminal subdomain is significantly higher than that for the N-terminus suggesting at least two regions of unfolding. At a more detailed level, there appears to be a broad continuum of stabilities throughout each region. The overall subdomain hierarchy of energies does not mirror data on the folding pathway for this protein, challenging the relationship between energy landscapes and folding trajectories.

引用

页码：1072 / 1078

页数：6