Solvent and mutation effects on the nucleation of amyloid β-protein folding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 51, 2005, Pages 18258-18263

  Cruz, Luis ^a   Urbanc, Brigita ^a   Borreguero, Jose M ^a,b   Lazo, Noel D ^c   Teplow, David B ^c   Stanley, H Eugene ^a  

^a Boston University   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alzheimer's disease; Hydrophobic interactions; Molecular dynamics; Salt bridges

Indexed keywords

AMYLOID BETA PROTEIN; ASPARTIC ACID; GLUTAMIC ACID; LYSINE; OLIGOMER; SOLVENT; VALINE; WATER;

ALZHEIMER DISEASE; AMINO ACID SUBSTITUTION; AMYLOIDOSIS; ARTICLE; BRAIN HEMORRHAGE; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLVATION;

AMYLOID BETA-PROTEIN; ELECTROSTATICS; HYDROPHOBICITY; LYSINE; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; VALINE;

EID: 29444439999     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0509276102     Document Type: Article

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