The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH

Rapid Communications in Mass Spectrometry

Volumn 26, Issue 16, 2012, Pages 1783-1792

  Hodkinson, John P ^a   Radford, Sheena E ^a   Ashcroft, Alison E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DYNAMICS; ETHANOL; FINANCE; GLYCOPROTEINS; PH; SELF ASSEMBLY; SODIUM COMPOUNDS; SULFUR COMPOUNDS; UREA;

AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; AMYLOID FORMATION; CONFORMATIONAL DYNAMICS; CONFORMATIONAL FLEXIBILITY; EXCHANGE RATES; HUMAN DISEASE; NEUTRAL PH; PROTEIN VARIANTS; WILD-TYPE PROTEINS;

PROTEINS;

EID: 84863644568     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.6282     Document Type: Review

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