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This book was planned and written with one central goal in mind: to
demonstrate that statistical thermodynamics can be used
successfully by a broad group of scientists, ranging from chemists
through biochemists to biologists, who are not and do not intend to
become specialists in statistical thermodynamics. The book is
addressed mainly to gradu ate students and research scientists
interested in designing experiments the results of which may be
interpreted at the molecular level, or in interpreting such
experimental results. It is not addressed to those who intend to
practice statistical thermodynamics per se. With this goal in mind,
I have expended a great deal of effort to make the book clear,
readable, and, I hope, enjoyable. This does not necessarily mean
that the book as a whole is easy to read. The first four chapters
are very detailed. The last four become progressively more
difficult to read, for several reasons. First, presuming that the
reader has already acquired familiarity with the methods and
arguments presented in the first part, I felt that similar
arguments could be skipped later on, leaving the details to be
filled in by the reader. Second, the systems themselves become
progressively more com plicated as we proceed toward the last
chapter.
This book deals with a subject that has been studied since the
beginning of physical chemistry. Despite the thousands of articles
and scores of books devoted to solvation thermodynamics, I feel
that some fundamen tal and well-established concepts underlying the
traditional approach to this subject are not satisfactory and need
revision. The main reason for this need is that solvation
thermodynamics has traditionally been treated in the context of
classical (macroscopic) ther modynamics alone. However, solvation
is inherently a molecular pro cess, dependent upon local rather
than macroscopic properties of the system. Therefore, the starting
point should be based on statistical mechanical methods. For many
years it has been believed that certain thermodynamic quantities,
such as the standard free energy (or enthalpy or entropy) of
solution, may be used as measures of the corresponding functions of
solvation of a given solute in a given solvent. I first challenged
this notion in a paper published in 1978 based on analysis at the
molecular level. During the past ten years, I have introduced
several new quantities which, in my opinion, should replace the
conventional measures of solvation thermodynamics. To avoid
confusing the new quantities with those referred to conventionally
in the literature as standard quantities of solvation, I called
these "nonconventional," "generalized," and "local" standard
quantities and attempted to point out the advantages of these new
quantities over the conventional ones."
My personal involvement with the problem of hydrophobic
interactions (HI) began about ten years ago. At that time I was
asked to write a review article on the properties of aqueous
solutions of nonpolar solutes. While surveying the literature on
this subject I found numerous discussions of the concept of HI. My
interest in these interactions increased especially after reading
the now classical review of W. Kauzmann (1959), in which the
importance of the HI to biochemical processes is stressed. Yet, in
spite of having read quite extensively on the various aspects of
the subject, I acquired only a very vague idea of what people
actually had in mind when referring to HI. In fact, it became quite
clear that the term HI was applied by different authors to describe
and interpret quite different phenomena occurring in aqueous
solutions. Thus, even the most fundamental question of the very
definition of the concept of HI remained unanswered. But other
questions followed, e. g.: Are HI really a well established
experimental fact? Is there any relation between HI and the
peculiar properties of water? Is the phenomenon really unique to
aqueous solutions? Finally, perhaps the most crucial question I
sought to answer was whether or not there exists hard evidence that
HI are really important -as often claimed-in biological processes."
This book evolved from a graduate course on applications of
statistical thermody- namics to biochemical systems. Most of the
published papers and books on this subject used in the course were
written by experimentalists who adopted the phenomenological
approach to describe and interpret their results. Two outstanding
papers that impressed me deeply were the c1assical papers by Monod,
Changeux, and Jacob (1963) and Monod, Wyman, and Changeux (1965),
where the allosteric model for regulatory enzymes was introduced.
Reading through them I feIt as if they were revealing one of the
c1everest and most intricate tricks of nature to regulate
biochemical processes. In 1985 I was glad to see T. L. HilI's
volume entitled Cooperativity Theory in Biochemistry, Steady State
and Equilibrium Systems. This was the fIrst book to systematically
develop the molecular or statistical mechanical approach to binding
systems. HilI demonstrated how and why the molecular approach is so
advanta- geous relative to the prevalent phenomenological approach
of that time. On page 58 he wrote the following (my italics): The
naturalness of Gibbs' grand partition function for binding problems
in biology is evidenced by the rediscovery of what is essentially
the grand partition function for this particular type of problem by
various physical biochentists, including E. Q. Adams, G.
This book evolved from a graduate course on applications of
statistical thermody- namics to biochemical systems. Most of the
published papers and books on this subject used in the course were
written by experimentalists who adopted the phenomenological
approach to describe and interpret their results. Two outstanding
papers that impressed me deeply were the c1assical papers by Monod,
Changeux, and Jacob (1963) and Monod, Wyman, and Changeux (1965),
where the allosteric model for regulatory enzymes was introduced.
Reading through them I feIt as if they were revealing one of the
c1everest and most intricate tricks of nature to regulate
biochemical processes. In 1985 I was glad to see T. L. HilI's
volume entitled Cooperativity Theory in Biochemistry, Steady State
and Equilibrium Systems. This was the fIrst book to systematically
develop the molecular or statistical mechanical approach to binding
systems. HilI demonstrated how and why the molecular approach is so
advanta- geous relative to the prevalent phenomenological approach
of that time. On page 58 he wrote the following (my italics): The
naturalness of Gibbs' grand partition function for binding problems
in biology is evidenced by the rediscovery of what is essentially
the grand partition function for this particular type of problem by
various physical biochentists, including E. Q. Adams, G.
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