The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity

Journal of Biological Chemistry

Volumn 281, Issue 52, 2006, Pages 39943-39952

  Basha, Eman ^a   Friedrich, Kenneth L ^a,b   Vierling, Elizabeth ^a  

^a UNIVERSITY OF ARIZONA   (United States)

^b PORTLAND COMMUNITY COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; DIMERS; ENZYME KINETICS; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; PLANTS (BOTANY);

CHAPERONE ACTIVITY; DENATURATION; INSOLUBILIZATION; MOLECULAR CHAPERONES;

PROTEINS;

ALPHA CRYSTALLIN; CHAPERONE; CITRATE SYNTHASE; FIREFLY LUCIFERASE; HEAT SHOCK PROTEIN; MALATE DEHYDROGENASE; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; COMPLEX FORMATION; ENZYME ACTIVITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SOLUBILIZATION;

ALPHA-CRYSTALLINS; AMINO ACID SEQUENCE; CITRATE (SI)-SYNTHASE; DIMERIZATION; HEAT; HEAT-SHOCK PROTEINS; LUCIFERASES; MALATE DEHYDROGENASE; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTANT CHIMERIC PROTEINS; PEAS; PEPTIDE FRAGMENTS; PLANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY; SUBSTRATE SPECIFICITY; TRITICUM;

EID: 33846018601     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M607677200     Document Type: Article

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