N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone

FEBS Journal

Volumn 280, Issue 11, 2013, Pages 2688-2699

  Tomar, Rachana ^a   Garg, Dushyant K ^a   Mishra, Rahul ^b   Thakur, Ashwani K ^b   Kundu, Bishwajit ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

Author keywords

amyloid; chaperone; domain; l asparaginase; protein aggregation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID BETA PROTEIN[1-42]; ASPARAGINASE; CHAPERONE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; GEL FILTRATION; HYDROPHOBICITY; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN REFOLDING; PROTEIN STABILITY; PYROCOCCUS FURIOSUS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEDIMENTATION; THERMOSTABILITY;

ASPARAGINASE; ENZYME STABILITY; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PYROCOCCUS FURIOSUS;

PYROCOCCUS FURIOSUS;

EID: 84878242705     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12271     Document Type: Article

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