- Abstract:
-
Changes in microscopic viscosity and macromolecular crowding accompany the transition of proteins from their monomeric forms into highly organised fibrillar states. Previously, we have demonstrated that viscosity sensitive fluorophores termed 'molecular rotors', when freely mixed with monomers of interest, are able to report on changes in microrheology accompanying amyloid formation, and measured an increase in rigidity of approximately three orders of magnitude during aggregation of lysozyme...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 1.6MB)
-
- Publisher copy:
- 10.1016/j.biomaterials.2017.06.009
-
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- Funding agency for:
- de Saint Victor, M
- Funding agency for:
- Stride, E
- Funding agency for:
- Kuimova, MK
- Publisher:
- Elsevier Publisher's website
- Journal:
- Biomaterials Journal website
- Volume:
- 139
- Pages:
- 195-201
- Publication date:
- 2017-06-07
- Acceptance date:
- 2017-06-05
- DOI:
- EISSN:
-
1878-5905
- ISSN:
-
0142-9612
- Pubs id:
-
pubs:702202
- URN:
-
uri:e66eed6f-f511-4a47-b106-94f6879c0525
- UUID:
-
uuid:e66eed6f-f511-4a47-b106-94f6879c0525
- Local pid:
- pubs:702202
- Language:
- English
- Keywords:
- Copyright holder:
- © 2017 Kubánková, et al. Published by Elsevier Ltd.
- Copyright date:
- 2017
- Notes:
-
Published by Elsevier Ltd. This is an open access article under the CC BY license
(http://creativecommons.org/licenses/by/4.0/).
Journal article
Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors
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