The Hydrophobic Effect

A unified overview of the dynamical properties of water and its unique and diverse role in biological and chemical processes.

A Top 25 CHOICE 2016 Title, and recipient of the CHOICE Outstanding Academic Title (OAT) Award. How much energy is released in ATP hydrolysis? How many mRNAs are in a cell? How genetically similar are two random people? What is faster, transcription or translation?Cell Biology by the Numbers explores these questions and dozens of others provid

This almost entirely rewritten edition remains the only comprehensive, up-to-date account of the subject available today—with nearly half of all literature references made to work done since 1973. Theoretical treatment of micelle formation has been greatly improved, making it possible to predict (from first principles) the size and size distribution of micelles formed by many simple amphiphiles . . . as well as the critical concentration at which they first form. Defines four distinct modes of association between protein and detergents (or other amphiphiles), and gives a plausible explanation to show why some ionic detergents generally denature proteins while nonionic detergents often do not. Also includes entirely new chapters on serum lipoproteins and on membrane proteins.

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 gives the reader an introduction to the field of surfactants in solution as well as polymers in solution. Starting with an introduction to surfactants the book then discusses their environmental and health aspects. Chapter 3 looks at fundamental forces in surface and colloid chemistry. Chapter 4 covers self-assembly and 5 phase diagrams. Chapter 6 reviews advanced self-assembly while chapter 7 looks at complex behaviour. Chapters 8 to 10 cover polymer adsorption at solid surfaces, polymers in solution and surface active polymers, respectively. Chapters 11 and 12 discuss adsorption and surface and interfacial tension, while Chapters 13- 16 deal with mixed surfactant systems. Chapter 17, 18 and 19 address microemulsions, colloidal stability and the rheology of polymer and surfactant solutions. Wetting and wetting agents, hydrophobization and hydrophobizing agents, solid dispersions, surfactant assemblies, foaming, emulsions and emulsifiers and microemulsions for soil and oil removal complete the coverage in chapters 20-25.

Provides deep insight into the concepts and recent developments in the area of supramolecular chemistry in water Written by experts in their respective field, this comprehensive reference covers various aspects of supramolecular chemistry in water?from fundamental aspects to applications. It provides readers with a basic introduction to the current understanding of the properties of water and how they influence molecular recognition, and examines the different receptor types available in water and the types of substrates that can be bound. It also looks at areas to where they can be applied, such as materials, optical sensing, medicinal imaging, and catalysis. Supramolecular Chemistry in Water offers five major sections that address important topics like water properties, molecular recognition, association and aggregation phenomena, optical detection and imaging, and supramolecular catalysis. It covers chemistry and physical chemistry of water; water-mediated molecular recognition; peptide and protein receptors; nucleotide receptors; carbohydrate receptors; and ion receptors. The book also teaches readers all about coordination compounds; self-assembled polymers and gels; foldamers; vesicles and micelles; and surface-modified nanoparticles. In addition, it provides in-depth information on indicators and optical probes, as well as probes for medical imaging. -Covers, in a timely manner, an emerging area in chemistry that is growing more important every day -Addresses topics such as molecular recognition, aggregation, catalysis, and more -Offers comprehensive coverage of everything from fundamental aspects of supramolecular chemistry in water to its applications -Edited by one of the leading international scientists in the field Supramolecular Chemistry in Water is a one-stop-resource for all polymer chemists, catalytic chemists, biochemists, water chemists, and physical chemists involved in this growing area of research.

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.