Chemist Kauzmann GS '40 dies at 92

A member of the Manhattan Project, Kauzmann studied the properties of water and supercooled liquids and also made discoveries in the ’50s concerning the hydrophobic effect and protein structure.

He discovered that the hydrophobic effect was the main driving force for protein folding: A protein tends to fold in on itself in a way that buries its greasy, water-averse regions in its interior.

Kauzmann made his findings without modern technology, relying only on fundamental principles to interpret his simple experiments.

“He understood the forces and interactions that caused proteins to fold even before one could see a picture of what the folded structure looks like,” Princeton protein researcher and chemistry professor Michael Hecht said.

“Anyone who works with proteins knows who Kauzmann is, because he was the guy who first came up with these really central ideas,” Hecht added.

Beyond his academic accomplishments, colleagues said they remember Kauzmann fondly for his distinctive personality. A family man, he enjoyed building catapults and making candied grapefruit rinds, which he gave to friends and relatives.

“When I first met Walter Kauzmann, I called him ‘Professor.’ He responded, ‘Don’t call me “Professor.” I would even rather have you call me “Walter” than that,’ ” said David Eisenberg, a chemistry professor at UCLA who studied with Kauzmann in the ’60s.

Kauzmann was also an avid outdoorsman, Eisenberg added.

“We went for a camping trip [with the Kauzmann family],” Eisenberg said. “At that time, I was having some back trouble, so although Kauzmann was 25 years older than I, he carried both his pack and mine.”

Thomas Spiro, a chemistry professor at the University of Washington, said he enjoyed going to dinner with Kauzmann. “His policy was to order dessert first because he said it was the best part of the meal,” Spiro said.

Spiro entered the Princeton chemistry department in 1963, six months before Kauzmann became the chair of the department.

Kauzmann was a “supportive” chairman, Spiro said, adding that he was “always accessible when you had a problem.”

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Kauzmann preferred to make his points with copious amounts of chalk dust, Spiro noted. “He loved to get on the blackboard and work from first principles,” he said.

Eisenberg also said he remembered Kauzmann as an encouraging and helpful mentor.

“Although a great scholar, he was unbelievably generous with his time, spending many hours a week with me, trying to puzzle out the atomic structure of liquid water,” Eisenberg said in an e-mail.

During his life, Kauzmann’s name became increasingly prominent in scientific circles: Students, especially in the field of protein research, frequently studied his work. Hecht was one of them.

“At that point, Kauzmann had written these paperback non-formal books,” Hecht said, adding, “We used those instead of a regular textbook in those courses.”

When Hecht entered the Princeton chemistry department in 1992, Kauzmann, who was in his early 70s then, had already retired.

Retirement did not mean inactivity for Kauzmann, who continued to share his acumen with others, Hecht said.

Even during his later years, Kauzmann would still be found in the corridors of Frick, talking to juniors about the latest chemistry news, Hecht said.

“You would see him all the time,” Hecht said. “He was still very much around.”