Identification of a conserved aggregation-prone intermediate state in the folding pathways of Spc-SH3 amyloidogenic variants

Journal of Molecular Biology

Volumn 422, Issue 5, 2012, Pages 705-722

  Krobath, H ^a   Estacio S G ^b   Faisca P F N ^a   Shakhnovich, E I ^c  

^a Centro de Fisica da Materia Condensada   (Portugal)

^b RESEARCH INSTITUTE FOR MEDICINES IMED ULISBOA   (Portugal)

^c HARVARD UNIVERSITY   (United States)

Author keywords

aggregation; amyloids; intermediate states; molecular dynamics; protein folding

Indexed keywords

AMYLOID PROTEIN; FODRIN; PROTEIN SH3; PROTEIN VARIANT;

ARTICLE; CONTROLLED STUDY; DIMERIZATION; HYDROPHOBICITY; IN VITRO STUDY; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MUTATION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING;

EID: 84865691204     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.020     Document Type: Article

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