Loading…
Revealing Conformational Variants of Solution‐Phase Intrinsically Disordered Tau Protein at the Single‐Molecule Level
Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution‐phase structural studies. We employed an anti‐Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we recorded the fluo...
Saved in:
Published in: | Angewandte Chemie 2017-12, Vol.129 (49), p.15790-15794 |
---|---|
Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution‐phase structural studies. We employed an anti‐Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we recorded the fluorescence anisotropy to investigate the diversity of conformations sampled by the single molecules. A distribution of anisotropy values obtained from trapped tau protein is conspicuously bimodal while those obtained by trapping a globular protein or individual fluorophores are not. Time‐resolved fluorescence anisotropy measurements were used to provide an explanation of the bimodal distribution as originating from a shift in the compaction of the two different families of conformations.
Eine Anti‐Brownsche elektrokinetische Falle wurde verwendet, um Messungen einzelner Tau‐Proteine in Lösung zu verlängern. Die unterschiedlichen Konformationen der einzelnen Moleküle wurden durch Fluoreszenzanisotropie bestimmt. Die Verteilung der Anisotropiewerte von gefangenem Tau‐Protein ist im Gegensatz zu denen von globularen Proteinen und einzelnen Fluorophoren auffällig bimodal. |
---|---|
ISSN: | 0044-8249 1521-3757 |
DOI: | 10.1002/ange.201708242 |