Kauzmann, Walter

Kato Tosio, 584,585 Kauzmann Walter, 796, 867 Kekule Friedrich August... 

In this section we shall briefly indicate the origin of some of the expressions governing optical activity that wiU be pertinent for our discussion later on. Our object in doing this is to refresh the reader s memory and, at the same time, to introduce our notation. In doing so, we shall draw heavily upon the excellent review articles of Condon and of Kauzmann, Walter and Eyring. No attempt at derivation will be essayed, and the more rigorous reader is referred to Condon s paper for many of the statements about to be made. 

L. deBroghe, The devolution in Phjsics, Noonday Press, Inc., New York, 1953 H. Eyring, J. Walter, and G. E. Kimball, Quantum Chemistj, ](Am. Wiley Sons, Inc., New York, 1944 W. Kauzmann, Quantum Chemistj, Academic Press, New York, 1957. 

Abstract. Walter Kauzmann stated in a review of protein thermodynamics that volume and enthalpy changes are equally fundamental properties of the unfolding process, and no model can be considered acceptable unless it accounts for the entire thermodynamic behaviour (Nature 325 763-764, 1987). While the thermodynamic basis for pressure effects has been known for some time, the molecular mechanisms have remained rather mysterious. We, and others in the rather small field of pressure effects on protein structure and stability, have attempted since that time to clarify the molecular and physical basis for the changes in volume that accompany protein conformational transitions, and hence to explain pressure effects on proteins. The combination of many years of work on a model system, staphylococcal nuclease and its large numbers of site-specific mutants, and the rather new pressure perturbation calorimetry approach has provided for the first time a fundamental qualitative understanding of AV of unfolding, the quantitative basis of which remains the goal of current work. 

Not all resisted the introduction of the new tool. I wish to acknowledge the very firm support and encouragement I got from Walter Kauzmann and John Edsal. They were the first to appreciate and grasp the advantage of a new tool and encouraged me to continue with its development. Today, I am proud,... 

Ever since Walter Kauzmann s searching analysis of hydro-phobic interactions ( 7), 20 years ago, the subject has been a major concern of protein chemists and others. Such interactions have been invoked to explain an immense range of phenomena. The interpretations were not always convincing, but the remarkable behavior of dilute solutions of hydrophobic compounds in water is compellingly clear. Here I aim only to note one aspect of these phenomena, which I think deserves more attention that it has received. I will consider only the properties of such systems at infinite dilution of solute. The already well-known features of these water-solute interactions are several. When a hydrophobic compound, or a compound... 

I have also profited from valuable discussions and correspondence with Walter Kauzmann, Seymour H. Koenig, I.D. 

We are grateful to Patricia Adams, for carrying out measurements of the enzymatic activity of lysozyme, and to Professor Walter Kauzmann for stimulation and critical discussions. This work was supported by NIH research grant GM-24760. 

Walter Kauzmann, Department of Chemistry, Princeton University, Princeton, New Jersey... 

In 1959, Walter J. Kauzmann (1916- ) at Princeton clarified the notions of "hydrophobic bonding" when he noted that water is actually attracted to hydrophobic molecules with a very small amount of heat released upon association. This is the result of nonbonding (van der Waals) attraction and in some cases (e.g., benzene) some... 

It is common knowledge that amphiphilic molecules, such as sodium dodecyl sulfate, above a certain critical concentration in water form assembled suiictures in which the hydrophobic units are clustered together. The notice of a hydrophobic effect was brought to light by Walter Kauzmann, whilst studying forces that influenced protein denaturation [27]. An excellent critical review on interfaces and the driving forces of hydrophobic assembly was written by Chandler in 2005 [28]. 

After I have finished proofreading this book, I heard the sad news about Walter Kauzmann s passing away on January 27, 2009. 

I met Walter Kauzmann in one of the first Gordon conferences on Water back in the late 1960 s. It was during our long walks through the woods of New Hampshire that he encouraged me to write my first book on Water and Aqueous Solutions, ... 

Press, Ithaca, 1948, where inter alia he elucidated the role of hydrogen bonds in forming structures. The hydrophobic effect was first highlighted by Walter Kauzmann in a paper Some Factors in the Interpretation of Protein... 

By Walter Kauzmann (1916-2009) in an early book, Quantum Chemistry, Academxc Press, New York, 1957. 

Walter Kauzmann (p. 42) was chairman of the Princeton University chemistry department in 1964 when MJ intertdewed for a job. He made this comment in response to a typically convoluted molecular orbital answer to some simple question. 

FIGURE 8.5 Prof. Walter J. Kauzmann (1916-2009) was an American physical chemist whose research spanned thermodynamics (Kauzmann s paradox of supercooled hquids), quantum chemistry (1957 text), and biochemistry (the hydrophobic effect in enzymes). He was the Chair of Chemistry at Princeton University from 1964 to 1968 and the Chair of the Department of Biochemistry from 1980 to 1981. He is probably best known for his work on the thermodynamics and optical activity of proteins. (From Princeton University Department of Chemistry. With permission.)... 

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