Proteins act as macromolecular machinery that mediate many diverse
biological processes - the molecular mechanisms of this machinery
has fascinated biologists for decades. Analysis of the kinetic and
thermodynamic features of these mechanisms could reveal
unprecedented aspects of how the machinery function and will
eventually lead to a novel understanding of various biological
processes. This dissertation comprehensively demonstrates how two
universally conserved guanosine triphosphatases in the signal
recognition particle and its membrane receptor maintain the
efficiency and fidelity of the co-translational protein targeting
process essential to all cells. A series of quantitative
experiments reveal that the highly ordered and coordinated
conformational states of the machinery are the key to their
regulatory function. This dissertation also offers a mechanistic
view of another fascinating system in which multistate protein
machinery closely control critical biological processes. Written
while completing graduate work at California Institute of
Technology.
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