Journal article
Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors
- Abstract:
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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...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 1.6MB)
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- Publisher copy:
- 10.1016/j.biomaterials.2017.06.009
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Authors
Funding
+ Engineering and Physical Sciences Research Council
More from this funder
Funding agency for:
de Saint Victor, M
Grant:
EP/G036861/1/
+ Research Council UK
More from this funder
Funding agency for:
de Saint Victor, M
Grant:
EP/G036861/1/
+ Engineering and Physical Sciences Research Council
More from this funder
Funding agency for:
Stride, E
Grant:
EP/G036861/1/
+ Engineering and Physical Sciences Research Council
More from this funder
Funding agency for:
Kuimova, M
Grant:
EP/I003983/1/
Bibliographic Details
- 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:
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1878-5905
- ISSN:
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0142-9612
- Source identifiers:
-
702202
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:702202
- UUID:
-
uuid:e66eed6f-f511-4a47-b106-94f6879c0525
- Local pid:
- pubs:702202
- Deposit date:
- 2017-08-04
Terms of use
- 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/).
- Licence:
- CC Attribution (CC BY)
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