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...

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Bibliographic Details
Main Authors: O'Donnell, Charles William, Waldispuhl, Jerome, Lis, Mieszko, Halfmann, Randal Arthur, Devadas, Srinivas, Lindquist, Susan, Berger Leighton, Bonnie
Other Authors: Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory
Format: Article
Language:en_US
Published: Oxford University Press 2011
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