Characterization of the isolated 20 kDa and 50 kDa fragments of the myosin head
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference39 articles.
1. Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains
2. The free heavy chain of vertebrate skeletal myosin subfragment 1 shows full enzymatic activity.
3. Protein Folding
4. Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin
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1. Isolating and Localizing ATP-Sensitive Tryptophan Emission in Skeletal Myosin Subfragment 1;Biochemistry;2000-08-31
2. The Region in Myosin S-1 that may be Involved in Energy Transduction;Mechanism of Myofilament Sliding in Muscle Contraction;1993
3. Inactivation, subunit dissociation, aggregation, and unfolding of myosin subfragment 1 during guanidine denaturation;Biochemistry;1992-02-01
4. A search for protein structural changes accompanying the contractile interaction.;Proceedings of the National Academy of Sciences;1991-11-01
5. The isolated 21 kDa N-terminal fragment of myosin binds to actin in an ATP and ionic strength-dependent manner;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1991-04
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