Amyloid fibril-like structure underlies the aggregate structure across the pH range for β-lactoglobulin

Biophysical Journal

Volumn 96, Issue 12, 2009, Pages 5013-5019

  Krebs, Mark R H ^a   Devlin, Glyn L ^a,b   Donald, Athene M ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b MONASH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA LACTOGLOBULIN; THIOFLAVINE;

ARTICLE; BETA SHEET; ELECTRON MICROSCOPY; INFRARED SPECTROSCOPY; ISOELECTRIC POINT; LIGAND BINDING; MOLECULAR DYNAMICS; MORPHOLOGY; PH; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

EID: 68949142908     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.03.028     Document Type: Article

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