R120G αB-crystallin promotes the unfolding of reduced α-lactalbumin and is inherently unstable

FEBS Journal

Volumn 272, Issue 3, 2005, Pages 711-724

  Treweek, Teresa M ^a   Rekas, Agata ^a   Lindner, Robyn A ^a,f   Walker, Mark J ^a   Aquilina, J Andrew ^a,b   Robinson, Carol V ^b   Horwitz, Joseph ^c   Der Perng, Ming ^d   Quinlan, Roy A ^d   Carver, John A ^a,e  

^a UNIVERSITY OF WOLLONGONG   (Australia)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c JULES STEIN EYE INSTITUTE   (United States)

^d DURHAM UNIVERSITY   (United Kingdom)

^e UNIVERSITY OF ADELAIDE   (Australia)

^f Proteome Systems Ltd   (Australia)

Author keywords

Cataract; Lens proteins; Molecular chaparone; Protein aggregation; Protein unfolding

Indexed keywords

ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; ARGININE; CHAPERONE; DESMIN; GLYCINE; LENS PROTEIN; MUTANT PROTEIN; UREA; CRYSTALLIN; LACTALBUMIN;

ARTICLE; CATARACT; GEL ELECTROPHORESIS; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; LIGHT SCATTERING; MASS SPECTROMETRY; MISSENSE MUTATION; MYOPATHY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; WILD TYPE; ANIMAL; CATTLE; CHEMISTRY; GEL CHROMATOGRAPHY; LIGHT; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHYSIOLOGY; PROTEIN DENATURATION; RADIATION SCATTERING;

GENETTA;

ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CRYSTALLINS; LACTALBUMIN; LIGHT; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; SCATTERING, RADIATION;

EID: 13444260973     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04507.x     Document Type: Article

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