This book presents a new view of the mechanism of functional expression
of ATP-driven motors (proteins or protein complexes). It is
substantially different from the prevailing idea that the motor converts
chemical energy to mechanical work. To facilitate understanding, the
differences between the new and prevailing views are explained using
many illustrations. The book is of interest to those who are not
convinced of the notion of chemo-mechanical coupling. The claims
presented are the following: The system, which comprises not only the
motor but also water, does no mechanical work during the ATP hydrolysis
cycle; a protein is moved or a protein in the complex is rotated by the
entropic force generated by water. The highlight of the explanation in
the book is that the mechanism of unidirectional rotation of the central
shaft in F1-ATPase is discussed in detail on the basis of
this new view. The hydration entropy of each β subunit to which a
specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound,
the hydration entropy of the α3β3 complex, and the
dependence of the hydration entropy of F1-ATPase on the
orientation of the γ subunit play essential roles.