Transition Path Times Measured by Single-Molecule Spectroscopy

JOURNAL OF MOLECULAR BIOLOGY

卷:430

Review

Chung, Hoi Sung¹ 

[1] NIDDK, Natl Inst Hlth, 5 Mem Dr, Bethesda, MD 20892 USA

关键词: protein folding;    nucleic acid folding;    energy landscape;    FRET;    force spectroscopy;   

DOI  :  10.1016/j.jmb.2017.05.018

来源: Elsevier

【 摘 要 】

The transition path is a tiny fraction of a molecular trajectory during which the free-energy barrier is crossed. It is a single-molecule property and contains all mechanistic information of folding processes of biomolecules such as proteins and nucleic acids. However, the transition path has been difficult to probe because it is short and rarely visited when transitions actually occur. Recent technical advances in single-molecule spectroscopy have made it possible to directly probe transition paths, which has opened up new theoretical and experimental approaches to investigating folding mechanisms. This article reviews recent single-molecule fluorescence and force spectroscopic measurements of transition path times and their connection to both theory and simulations. Published by Elsevier Ltd.

【 授权许可】

Free