| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2049107 | FEBS Letters | 2008 | 6 Pages |
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 °C, Hsp27 effectively suppresses S1 aggregation, and this effect is enhanced by mutations mimicking Hsp27 phosphorylation. However, Hsp27 was unable to prevent thermal unfolding of myosin heads and to maintain their ATPase activity under heat-shock conditions.Structured summaryMINT-6490863, MINT-6490872:LC1 (S1) (uniprotkb:P02602), Myosin subfragment 1 (S1) (uniprotkb:P02562) and Hsp27 (uniprotkb:P04792) physically interact (MI:0218) by dynamic light scattering (MI:0038)MINT-6490833:LC1 (S1) (uniprotkb:P02602), Myosin subfragment 1 (S1) (uniprotkb:P02562) and Hsp27 (uniprotkb:P04792) physically interact (MI:0218) by cosedimentation (MI:0027)MINT-6490770, MINT-6490782:LC1 (S1) (uniprotkb:P02602), Myosin subfragment 1 (S1) (uniprotkb:P02562) and Hsp27 (uniprotkb:P04792) physically interact (MI:0218) by light scattering (MI:0067)
