Fluorescence quenching: A tool for single-molecule protein-folding study.

Abstract:

:By using titin as a model system, we have demonstrated that fluorescence quenching can be used to study protein folding at the single molecule level. The unfolded titin molecules with multiple dye molecules attached are able to fold to the native state. In the native folded state, the fluorescence from dye molecules is quenched due to the close proximity between the dye molecules. Unfolding of the titin leads to a dramatic increase in the fluorescence intensity. Such a change makes the folded and unfolded states of a single titin molecule clearly distinguishable and allows us to measure the folding dynamics of individual titin molecules in real time. We have also shown that fluorescence quenching can signal folding and unfolding of a small protein with only one immunoglobulin domain.

authors

Zhuang X,Ha T,Kim HD,Centner T,Labeit S,Chu S

doi

10.1073/pnas.97.26.14241

keywords:

subject

Has Abstract

pub_date

2000-12-19 00:00:00

pages

14241-4

issue

26

eissn

0027-8424

issn

1091-6490

pii

97/26/14241

journal_volume

97

pub_type

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