The relevance of silks to amyloids
(2010) p.51-70- Abstract
- At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies... (More)
- At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies within fibre-forming proteins research. (Less)
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https://lup.lub.lu.se/record/7c4bcaaa-f0a8-44c6-92a0-6b23685048c1
- author
- Dicko, Cedric LU ; Porter, David and Vollrath, Fritz
- publishing date
- 2010
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- host publication
- Functional Amyloid Aggregation
- editor
- Riggaci, Stefania and Bucciantini, Monica
- pages
- 20 pages
- publisher
- Research Signpost
- ISBN
- 978-81-308-0425-5
- language
- English
- LU publication?
- no
- id
- 7c4bcaaa-f0a8-44c6-92a0-6b23685048c1
- date added to LUP
- 2020-06-11 10:35:35
- date last changed
- 2021-04-08 09:11:13
@inbook{7c4bcaaa-f0a8-44c6-92a0-6b23685048c1, abstract = {{At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies within fibre-forming proteins research.}}, author = {{Dicko, Cedric and Porter, David and Vollrath, Fritz}}, booktitle = {{Functional Amyloid Aggregation}}, editor = {{Riggaci, Stefania and Bucciantini, Monica}}, isbn = {{978-81-308-0425-5}}, language = {{eng}}, pages = {{51--70}}, publisher = {{Research Signpost}}, title = {{The relevance of silks to amyloids}}, year = {{2010}}, }