title: On the origin and transmission of force in actomyosin subfragment 1.
abstract: A proximity map showing the three-dimensional arrangement of 12 chemically defined points in actomyosin subfragment 1 is developed and roughly correlated with published electron microscope reconstruction of others. Several additional points and topological relationships in the primary polypeptide chain folding are assimilated into this model. Certain crosslinkings and distance change observations are interpreted as indicators of transmission of force/displacement between the nucleotide-binding and an actin-binding site--i.e., as indications of how energy is transduced in this system.
authors.affiliation: Cardiovascular Research Institute, University of California, San Francisco 94143.
authors.forename: J
authors.initials: J
authors.lastname: Botts
authors.forename: J F
authors.initials: JF
authors.lastname: Thomason
authors.forename: M F
authors.initials: MF
authors.lastname: Morales
mesh_terms: D008854:Microscopy, Electron / Q000379:methods; D008962:Models, Theoretical; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins