A method for probing the mutational landscape of amyloid structure | Zendy

Colm P. O’Donnell | Zendy; Jérôme Waldispühl | Zendy; Mieszko Lis | Zendy; Randal Halfmann | Zendy; Srinivas Devadas | Zendy; Susan Lindquist | Zendy; Bonnie Berger | Zendy

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A method for probing the mutational landscape of amyloid structure

Author(s) -

Colm P. O’Donnell,

Jérôme Waldispühl,

Mieszko Lis,

Randal Halfmann,

Srinivas Devadas,

Susan Lindquist,

Bonnie Berger

Publication year - 2011

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btr238

Subject(s) - mutant , amyloid (mycology) , mutagenesis , mutation , sequence (biology) , fibril , computational biology , amyloid disease , protein folding , amyloid fibril , protein structure , biophysics , chemistry , biology , biochemistry , amyloid β , gene , medicine , inorganic chemistry , disease , pathology

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 mutations can drastically alter amyloid function and pathogenicity. Experimental structure determination has proven extremely difficult with only a handful of NMR-based models proposed, suggesting a need for computational methods.

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