Myosin: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
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The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis. | The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis. | ||
{{Clear}} | {{Clear}} | ||
==Function== | ==Function== | ||