Characterization of Aβ aggregation mechanism probed by congo red

Journal of Biomolecular Structure and Dynamics

Volumn 30, Issue 2, 2012, Pages 160-169

  Wang, Chih Ching ^a   Huang, Hsien Bin ^b   Tsay, Huey Jen ^a   Shiao, Ming Shi ^c   Wu, Wen Jin Winston ^d   Cheng, Yi Cheng ^e   Lin, Ta Hsien ^a,f  

^a NATIONAL YANG MING UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

^c CHANG GUNG UNIVERSITY   (Taiwan)

^d INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^e MACKAY MEDICAL COLLEGE   (Taiwan)

^f TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

Author keywords

amyloid peptide; Congo red; Discordant helix; Nuclear magnetic resonance

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; CONGO RED; DODECYL SULFATE SODIUM;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; MOLECULAR INTERACTION; MOLECULAR MECHANICS; MOLECULAR PROBE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMYLOID BETA-PEPTIDES; BINDING SITES; CONGO RED; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84863880056     PISSN: 07391102     EISSN: None     Source Type: Journal    
DOI: 10.1080/07391102.2012.677767     Document Type: Article

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