One way in which cells maintain
spatial organization is through motor proteins that bind cargo and
move it along networks of cytoskeletal filaments. These
proteins—myosins, kinesins, dynein among others—exist in a host
of different forms, and we are interested in the common structural
design principles behind their dynamics. What explains a motor's
transport efficiency, its perseverance under load, its distribution
of step sizes and binding locations? By altering elements of their
structure, can we bioengineer motors toward specific biomedical
applications?
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