A Structural Model for Apolipoprotein C-II Amyloid Fibrils: Experimental Characterization and Molecular Dynamics Simulations

• Published in: Journal of molecular biology Vol. 405; no. 5; pp. 1246 - 1266
• Main Authors: Teoh, Chai Lean, Pham, Chi L.L., Todorova, Nevena, Hung, Andrew, Lincoln, Craig N., Lees, Emma, Lam, Yuen Han, Binger, Katrina J., Thomson, Neil H., Radford, Sheena E., Smith, Trevor A., Müller, Shirley A., Engel, Andreas, Griffin, Michael D.W., Yarovsky, Irene, Gooley, Paul R., Howlett, Geoffrey J.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 04.02.2011
• Subjects: Amino Acid Sequence; Amyloid - chemistry; Amyloid - ultrastructure; Apolipoprotein C-II - chemistry; atomic force microscopy; cross-β-structure; fluorescence resonance energy transfer; Humans; Microscopy, Atomic Force; Models, Chemical; Molecular Dynamics Simulation; Molecular Sequence Data; Protein Structure, Secondary; scanning transmission electron microscopy; Sequence Analysis, Protein; X-Ray Diffraction; ThT; SPC; X-ray diffraction; fluorescence resonance energy transfer; AFM; MPL; TCSPC; cross-β-structure; atomic force microscopy; 1,5-I-AEDANS; STEM; MD; scanning transmission electron microscopy; FRET; apoC-II; H/D; TEM; GuHCl

The self-assembly of specific proteins to form insoluble amyloid fibrils is a characteristic feature of a number of age-related and debilitating diseases. Lipid-free human apolipoprotein C-II (apoC-II) forms characteristic amyloid fibrils and is one of several apolipoproteins that accumulate in amyl...