Amyloid formation under physiological conditions proceeds via a native-like folding intermediate

Nature Structural and Molecular Biology

Volumn 13, Issue 3, 2006, Pages 195-201

  Jahn, Thomas R ^a   Parker, Martin J ^a   Homans, Steve W ^a   Radford, Sheena E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; PROLINE;

AMYLOIDOSIS; ARTICLE; BETA SHEET; CONCENTRATION (PARAMETERS); CORRELATION ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN STRUCTURE; SPECIES DIFFERENCE; STRUCTURE ANALYSIS; TEMPERATURE; TRANS ISOMER;

AMINO ACIDS; AMYLOID; BETA 2-MICROGLOBULIN; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE; TIME FACTORS;

EID: 33144467755     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1058     Document Type: Article

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