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Article

Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation.

FEBS letters - 30 Apr 2008

Markov Denis I, Pivovarova Anastasia V, Chernik Ivan S, Gusev Nikolai B, Levitsky Dmitrii I

Abstract excerpt

We applied different methods, such as turbidity measurements, dynamic light scattering, differential scanning calorimetry and co-sedimentation assay, to analyze the interaction of small heat shock protein Hsp27 with isolated myosin head (myosin subfragment 1, S1) under heat-stress conditions. Upon heating at 43 degrees C, Hsp27 effectively suppresses S1 aggregation, and this effect is enhanced by mutations...

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Identifiers

PMID: 18387368
DOI: 10.1016/j.febslet.2008.03.035

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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