The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures

Structure

Volumn 9, Issue 2, 2001, Pages 83-91

  Mackay, Joel P ^a   Matthews, Jacqueline M ^a   Winefield, Robert D ^b,c   Mackay, Lindsey G ^d   Haverkamp, Richard G ^b   Templeton, Matthew D ^c  

^a UNIVERSITY OF SYDNEY   (Australia)

^b MASSEY UNIVERSITY   (New Zealand)

^c THE NEW ZEALAND INSTITUTE FOR PLANT AND FOOD RESEARCH LIMITED   (New Zealand)

^d NATIONAL HEALTH AND MEDICAL RESEARCH COUNCIL   (Australia)

Author keywords

Amphipathic monolayer; EAS, hydrophobin; Neurospora crassa; Self assembly

Indexed keywords

AMYLOID; CONGO RED; HYDROPHOBIN;

AQUEOUS SOLUTION; ARTICLE; BETA SHEET; BIREFRINGENCE; CONTROLLED STUDY; DISULFIDE BOND; NEUROSPORA CRASSA; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMYLOID; CIRCULAR DICHROISM; COLORING AGENTS; CONGO RED; FUNGAL PROTEINS; MOLECULAR SEQUENCE DATA; NEUROSPORA CRASSA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

NEUROSPORA CRASSA;

EID: 0035089501     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00559-1     Document Type: Article

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