Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22

被引：35
作者：
Kazakov, Alexey S. [1 ]
Markov, Denis I. [1 ]
Gusev, Nikolai B. [2 ]
Levitsky, Dmitrii I. [1 ,3 ]
机构：
[1] Russian Acad Sci, AN Bach Inst Biochem, Moscow 119071, Russia
[2] Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow, Russia
[3] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Moscow, Russia
来源：
BIOPHYSICAL CHEMISTRY | 2009年 / 145卷 / 2-3期
基金：
俄罗斯基础研究基金会;
关键词：
Small heat shock proteins; Intrinsically disordered proteins; Thermal unfolding; Downhill folding; Differential scanning calorimetry; Tryptophan fluorescence; ALPHA-CRYSTALLIN; INDUCED AGGREGATION; H11; ACTIN; HSPB8; FLUORESCENCE; DENATURATION; MUSCLE; MODEL;
D O I：
10.1016/j.bpc.2009.09.003
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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收藏
页码：79 / 85
页数：7
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