文章基本信息

标题：Full distance-resolved folding energy landscape of one single protein molecule
本地全文：下载
作者：J. Christof M. Gebhardt ; Thomas Bornschlögl ; Matthias Rief 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2010
卷号：107
期号：5
页码：2013-2018
DOI：10.1073/pnas.0909854107
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Kinetic bulk and single molecule folding experiments characterize barrier properties but the shape of folding landscapes between barrier top and native state is difficult to access. Here, we directly extract the full free energy landscape of a single molecule of the GCN4 leucine zipper using dual beam optical tweezers. To this end, we use deconvolution force spectroscopy to follow an individual molecule's trajectory with high temporal and spatial resolution. We find a heterogeneous energy landscape of the GCN4 leucine zipper domain. The energy profile is divided into two stable C-terminal heptad repeats and two less stable repeats at the N-terminus. Energies and transition barrier positions were confirmed by single molecule kinetic analysis. We anticipate that deconvolution sampling is a powerful tool for the model-free investigation of protein energy landscapes.
关键词：leucine zipper ; force spectroscopy ; optical tweezers ; protein folding ; deconvolution