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Small heat shock protein Hsp27 protects myosin S1 from heat‐induced aggregation, but not from thermal denaturation and ATPase inactivation
Author(s) -
Markov Denis I.,
Pivovarova Anastasia V.,
Chernik Ivan S.,
Gusev Nikolai B.,
Levitsky Dmitrii I.
Publication year - 2008
Publication title -
febs letters
Language(s) - Slovak
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.035
Subject(s) - hsp27 , myosin , heat shock protein , biophysics , atpase , chemistry , shock (circulatory) , heat shock , myosin head , denaturation (fissile materials) , protein aggregation , hsp70 , biochemistry , myosin light chain kinase , enzyme , biology , medicine , nuclear chemistry , gene
MINT‐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)