A Simulated Intermediate State for Folding and Aggregation Provides Insights into ΔN6 β2-Microglobulin Amyloidogenic Behavior

PLoS Computational Biology

Volumn 10, Issue 5, 2014, Pages

  Estácio, Sílvia G ^a   Krobath, Heinrich ^a   Vila Viçosa, Diogo ^b   Machuqueiro, Miguel ^b   Shakhnovich, Eugene I ^c   Faísca, Patrícia F N ^a  

^a Centro de Fisica da Materia Condensada   (Portugal)

^b UNIVERSITY OF LISBON   (Portugal)

^c HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PH;

AMYLOID PLAQUES; AMYLOIDOGENICITY; COMPUTATIONAL STUDIES; DIALYSIS-RELATED AMYLOIDOSIS; EX-VIVO; FOLDINGS; INTERMEDIATE STATE; N-TERMINALS; TERMINAL RESIDUES; WILD TYPES;

DIMERS;

AMYLOID; BETA 2 MICROGLOBULIN; AMYLOID PROTEIN; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

ACIDIFICATION; AMINO TERMINAL SEQUENCE; ARTICLE; DIMERIZATION; MATHEMATICAL COMPUTING; MOLECULAR MODEL; PROTEIN AGGREGATION; PROTEIN CLEAVAGE; PROTEIN FOLDING; PROTEIN STRUCTURE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

AMYLOIDOGENIC PROTEINS; BETA 2-MICROGLOBULIN; BINDING SITES; COMPUTER SIMULATION; DIMERIZATION; MODELS, CHEMICAL; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 84901650117     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003606     Document Type: Article

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