Influence of aggregation propensity and stability on amyloid fibril formation as studied by fourier transform infrared spectroscopy and two-dimensional COS analysis

Biochemistry

Volumn 48, Issue 44, 2009, Pages 10582-10590

  Cerdà Costa, Núria ^a   De La Arada, Igor ^b   Avilés, Francesc X ^a   Arrondo, José L R ^b   Villegas, Sandra ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION DOMAIN; AGGREGATION PROPENSITY; ALZHEIMER'S; AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; AMYLOIDOGENESIS; FIBRIL FORMATION; FINAL STATE; FOLDED STATE; MISFOLDING; SPONGIFORM ENCEPHALOPATHIES; TEM; WILD TYPES;

FOURIER TRANSFORM INFRARED SPECTROSCOPY; SPECTROSCOPIC ANALYSIS; SPECTROSCOPY; TRANSMISSION ELECTRON MICROSCOPY;

GLYCOPROTEINS;

AMYLOID; PROCARBOXYPEPTIDASE A2; UNCLASSIFIED DRUG;

ARTICLE; HUMAN; INFRARED SPECTROSCOPY; KINETICS; MUTANT; PRIORITY JOURNAL; PROTEIN AGGREGATION; TEMPERATURE; TRANSMISSION ELECTRON MICROSCOPY; WILD TYPE;

AMYLOID; CARBOXYPEPTIDASES A; CIRCULAR DICHROISM; ENZYME ACTIVATION; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MUTATION; PROTEIN FOLDING; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

EID: 70449437082     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900960s     Document Type: Article

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