A method for probing the mutational landscape of amyloid structure
Motivation: Proteins of all kinds can self-assemble into highly ordered β-sheet aggregates known as amyloid fibrils, important both biologically and clinically. However, the specific molecular structure of a fibril can vary dramatically depending on sequence and environmental conditions, and mutatio...
Main Authors: | , , , , , , |
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Other Authors: | |
Format: | Article |
Language: | en_US |
Published: |
Oxford University Press
2011
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Online Access: | http://hdl.handle.net/1721.1/65075 https://orcid.org/0000-0001-8253-7714 https://orcid.org/0000-0003-1307-882X https://orcid.org/0000-0002-2724-7228 |