Cited by 43Heat shock proteins researchProtein Structure and DynamicsProtein Interaction Studies and Fluorescence Analysis

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

Kazakov, Alexey S., Markov, Denis I., Gusev, Nikolai B., Levitsky, Dmitrii I.·2009·Biophysical Chemistry

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 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.

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Crossref · 10.1016/j.bpc.2009.09.003

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Authors
Kazakov, A. S., Markov, D. I., Gusev, N. B., & Levitsky, D. I.
Affiliations
  • Russian Academy of Sciences (RU)
  • Lomonosov Moscow State University (RU)
Corresponding author
Levitsky, Dmitrii I.
Venue
Biophysical Chemistry
Publisher
Elsevier BV
Published
2009-12
Volume
145
Issue
2-3
Pages
79-85
ISSN
0301-4622 (ISSN-L)
OpenAlex
W2109864603
Cited by
43
References
39
Citations by year
2026: 1 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2018: 3 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 5 · 2012: 7
FWCI
2.15
Type
journal article
Language
en
Open access
closed
Locations
  • Biophysical Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
Russian Academy of Sciences
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
Hsp22, small heat shock proteins, intrinsically disordered proteins, thermal denaturation, protein folding, alpha-crystallin domain, downhill folding, alpha-helix content, β-sheet content, intrinsic fluorescence, protein structure
MeSH terms
Actins, Calorimetry, Differential Scanning, Hot Temperature, Heat-Shock Proteins, Humans, Mutation, Protein Binding, Protein Denaturation, Protein Serine-Threonine Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Molecular Chaperones, alpha-Crystallins

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