Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates

Journal of Molecular Biology

Volumn 425, Issue 7, 2013, Pages 1158-1171

  Natalello, Antonino ^a,b   Mattoo, Rayees U H ^c   Priya, Smriti ^c   Sharma, Sandeep K ^c   Goloubinoff, Pierre ^c   Doglia, Silvia M ^a,b  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b INFM   (Italy)

^c UNIVERSITY OF LAUSANNE   (Switzerland)

Author keywords

chaperone substrate; luciferase; misfolded monomer; protein aggregation; rhodanese

Indexed keywords

HEAT SHOCK PROTEIN 70; LUCIFERASE; MONOMER; PROTEIN DNAK; THIOFLAVINE; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; BETA SHEET; CONFORMATION; FLUORESCENCE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

EID: 84875212796     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.12.025     Document Type: Article

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