The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity

Protein Science

Volumn 8, Issue 1, 1999, Pages 174-179

  Yang, Hongmei ^a   Huang, Sufang ^a   Dai, Hongzheng ^a   Gong, Yandao ^a   Zheng, Changxue ^a   Chang, Zengyi ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Chaperone activity; Conformational flexibility; Hsp16.3; Hydrophobic exposure

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALPHA CRYSTALLIN; BACTERIAL PROTEIN; CHAPERONE; DITHIOTHREITOL; GUANIDINE; HEAT SHOCK PROTEIN; INSULIN; MEMBRANE PROTEIN; UREA;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; HEATING; HYDROPHOBICITY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 0032898210     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.1.174     Document Type: Article

References (14)

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