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Solid‐State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well‐Ordered β‐Sheet Core Amidst Structural Heterogeneity
Author(s) -
Morris Vanessa K.,
Linser Rasmus,
Wilde Karyn L.,
Duff Anthony P.,
Sunde Margaret,
Kwan Ann H.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201205625
Subject(s) - hydrophobin , context (archaeology) , amyloid (mycology) , amyloid fibril , amphiphile , chemistry , nuclear magnetic resonance spectroscopy , monolayer , crystallography , copolymer , polymer science , biophysics , biochemistry , stereochemistry , biology , organic chemistry , medicine , amyloid β , polymer , pathology , inorganic chemistry , paleontology , disease , gene
GrEASy fibrils : Hydrophobins are fungal proteins that assemble into an amphipathic fibrillar monolayer with amyloid properties and a hydrophobic face as water‐resistant as Teflon. Solid‐state NMR studies on EAS hydrophobin fibrils reveal direct evidence of a partial molecular rearrangement on assembly and an ordered β‐sheet‐rich core in the context of a whole protein in this functional amyloid.