Site-directed mutations within the core 'α-crystallin' domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions

Journal of Molecular Biology

Volumn 289, Issue 2, 1999, Pages 397-411

  Muchowski, Paul J ^a   Wu, Gabrielle J S ^a   Liang, Jack J N ^c   Adman, Elinor T ^a   Clark, John I ^a,b  

^a UNIVERSITY OF WASHINGTON   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Core crystallin domain; Molecular chaperone; Protein structure; Small heat shock proteins; B crystallin

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CELL VIABILITY; CIRCULAR DICHROISM; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; HUMAN; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; SPECTROSCOPY; ULTRAVIOLET RADIATION;

ESCHERICHIA COLI;

EID: 0033522885     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2759     Document Type: Article

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