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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...
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Published in: | Angewandte Chemie International Edition 2017-12, Vol.56 (49), p.15584-15588 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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.
An anti‐Brownian electrokinetic trap was employed to prolong measurements of single tau proteins in solution. Once trapped, the fluorescence anisotropy was recorded to investigate the diversity of conformations sampled by the single molecules. The 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. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201708242 |