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Archives of Biochemistry and Biophysics

Volumn 514, Issue 1-2, 2011, Pages 27-32

Substituted tryptophans at amyloid-β(1-40) residues 19 and 20 experience different environments after fibril formation

(4) McDonough, Ryan T a Paranjape, Geeta a Gallazzi, Fabio b Nichols, Michael R a

a UNIVERSITY OF MISSOURI ST LOUIS (United States)

b UNIVERSITY OF MISSOURI (United States)

Author keywords

Aggregation; Amyloid beta protein; Fibrils; Tryptophan fluorescence

Indexed keywords

ACRYLAMIDE; AMYLOID; AMYLOID BETA PROTEIN[1-40]; MONOMER; POTASSIUM IODIDE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; AMYLOIDOSIS; ARTICLE; CONTROLLED STUDY; FIBER; FLUORESCENCE; KINETICS; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; SENILE PLAQUE; TRANSMISSION ELECTRON MICROSCOPY;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; FLUORESCENCE; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; TRYPTOPHAN;

EID: 84860388911 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2011.07.018 Document Type: Article

Times cited : (6)

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