NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: Differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ

Biochemical Journal

Volumn 437, Issue 3, 2011, Pages 493-503

  Williams, Danielle M ^a,b   Ecroyd, Heath ^a,c   Goodwin, Katy L ^a,b   Dai, Huanqin ^d   Fu, Haian ^e   Woodcock, Joanna M ^b   Zhang, Lixin ^d   Carver, John A ^a  

^a UNIVERSITY OF ADELAIDE   (Australia)

^b CENTRE FOR CANCER BIOLOGY   (Australia)

^c UNIVERSITY OF WOLLONGONG   (Australia)

^d INSTITUTE OF MICROBIOLOGY   (China)

^e EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

14 3 3 protein; Biophysical characterization; C terminal flexibility; Molecular chaperone; Protein aggregation; Protein protein interaction

Indexed keywords

CHAPERONE; PHOSPHOSERINE; SMALL HEAT SHOCK PROTEIN; STRATIFIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; GENETIC CONSERVATION; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; THERMODYNAMICS;

14-3-3 PROTEINS; AMINO ACID SEQUENCE; ESCHERICHIA COLI; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PHOSPHOSERINE; PROTEIN BINDING; TWO-HYBRID SYSTEM TECHNIQUES;

MAMMALIA;

EID: 79960274257     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20102178     Document Type: Article

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