Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22 |
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Authors: | Alexey S. Kazakov Denis I. Markov Nikolai B. Gusev Dmitrii I. Levitsky |
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Affiliation: | aA. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prosp. 33, 119071 Moscow, Russia;bDepartment of Biochemistry, School of Biology, Moscow State University, Russia;cA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia |
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Abstract: | 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 °C to 80 °C and above), and this is accompanied by complete disappearance of α-helices, significant decrease in β-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 α-crystallin domain) retaining folded structure and undergoing reversible thermal unfolding. The results are also discussed in terms of downhill folding scenario. |
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Keywords: | Small heat shock proteins Intrinsically disordered proteins Thermal unfolding Downhill folding Differential scanning calorimetry Tryptophan fluorescence |
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