Solid‐State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well‐Ordered β‐Sheet Core Amidst Structural Heterogeneity | Zendy

Morris Vanessa K. | Zendy; Linser Rasmus | Zendy; Wilde Karyn L. | Zendy; Duff Anthony P. | Zendy; Sunde Margaret | Zendy; Kwan Ann H. | Zendy

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research