Journal
BIOPHYSICAL CHEMISTRY
Volume 145, Issue 2-3, Pages 79-85Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2009.09.003
Keywords
Small heat shock proteins; Intrinsically disordered proteins; Thermal unfolding; Downhill folding; Differential scanning calorimetry; Tryptophan fluorescence
Funding
- Russian Foundation for Basic Research
- Program Molecular and Cell Biology of the Russian Academy of Sciences
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We applied different methods (differential scanning calorimetry, circular dichroism, Fourier transform infrared spectroscopy, and intrinsic fluorescence) to investigate the thermal-induced changes in the structure of small heat shock protein Hsp22. It has been shown that this protein undergoes thermal-induced unfolding that occurs within a very broad temperature range (from 27 degrees C to 80 degrees C and above), and this is accompanied by complete disappearance of alpha-helices, significant decrease in beta-sheets content, and by pronounced changes in the intrinsic fluorescence. The results confirm predictions that Hsp22 belongs to the family of intrinsically disordered proteins (IDP) with certain parts of its molecule (presumably, in the alpha-crystallin domain) retaining folded structure and undergoing reversible thermal unfolding. The results are also discussed in terms of downhill folding scenario. (C) 2009 Elsevier B.V. All rights reserved.
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