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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/20890


Title: Heat treatment of small heat shock proteins α-crystallin and Hsp16.3: structural changes vs. chaperone-like activity
Authors: Qilong, Mao
Danxia, Ke
Zengyi, Chang
Keywords: chaperone activity; heat treatment; small heat shock protein
Issue Date: 31-Dec-2001
Publisher: Tsinghua University, China
Citation: Tsinghua Science and Technology (ISSN: 1007-0212) Vol 6 Num 5
Abstract: Both α-crystallin from bovine eye lens and Hsp16.3 from Mycobacterium tuberculosis are members of the small heat shock protein family. They were preincubated at 100°C for 15 min and then cooled on ice immediately. The chaperone-like activities of preheated proteins were measured at 37° using DTT-treated insulin B chains as substrates. Both preheated proteins exhibited greatly enhanced chaperone-like activities, accompanied with almost unchanged secondary structures and surface hydrophobicity but with a minor change in tertiary structures. The dramatically enhanced chaperone-like activities of preheated a-crystallin and Hsp16.3 may have resulted from the irreversible change in the tertiary structure as detected by near-UV CD spectra.
URI: http://hdl.handle.net/1807/20890
Other Identifiers: http://www.bioline.org.br/abstract?id=ts01088
Rights: Copyright 2001 - Tsinghua Science and Technology
Appears in Collections:Bioline International Legacy Collection

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