Over his remarkable 40-year career, Goldenberg would become not only a distinguished researcher at the forefront of biophysical chemistry but also a devoted educator who helped shape the undergraduate experience for countless students.

His colleague David Blair, who first met Goldenberg in 1990 during his own faculty interview, remembers being picked up at the airport by his future colleague. “We went for a beer,” Blair recalls. “We talked about the thermodynamics of water. It’s not a typical over-the-beer conversation, but it was fun.”

That conversation was quintessentially Goldenberg—a scientist inspired by the fundamental forces that govern life itself.

At the Physical Edge of Biology

The School of Biological Sciences is one of the largest academic units at the U with interests and programs spanning from molecular biophysics to global ecology and Goldenberg occupied a unique position as “the extreme biophysical end of the department” which in 2018 became a school. To illustrate this point during his retirement tribute in May 2025, Blair shared a quote from one of Goldenberg’s papers: “In the context of pure populations, the product operators are shown to represent quantum correlations between the nuclei and individual molecules, and a new variation on the classical vector diagram is introduced to represent these correlations.”

“Very biophysical. It has to do with NMR,” Blair explains. “The joke was, who understands this, right? And I knew literally no one in the audience would truly understand that.”

Yet this technical sophistication never isolated Goldenberg from his colleagues. “He’s always been a natural fit,” Blair notes, “in spite of his very physical character, in the sense that he also has an appreciation for genetics and evolution.”

Master of Mutations and Disulfide Bonds

Goldenberg’s research focus on protein folding—understanding how linear chains of amino acids fold into specific three-dimensional structures that determine function — was groundbreaking in its approach. He became “well known for” using “genetic approaches to studying protein folding,” as Blair puts it, citing another paper: “Mutational analysis of a protein folding pathway … destabilizing amino acid replacements at different sites in the protein can have distinct effects on the kinetics and equilibria of different steps in a protein folding reaction.”

“That’s almost plain English,” Blair observes with a smile. “It’s accessible to everyone.”

Goldenberg’s work often centered on bovine pancreatic trypsin inhibitor (BPTI), a small but well-folded protein stabilized by multiple disulfide bonds. These chemical linkages provided what Blair describes as “tools” and “access to the folding pathway,” because they form at different rates during folding and contribute differently to protein stability. This work made Goldenberg “very expert in the chemistry of thiol disulfide equilibrium reactions.”

A Career Spanning Revolutionary Change

Goldenberg’s career coincided with an explosion in structural biology. As Blair notes, “When he was three years old, the first protein structure was solved” — myoglobin, determined by X-ray crystallography and worthy of a Nobel Prize. “When he came here, there were 150 protein structures known. And now, after his 40-year career, there are more than 200,000 protein structures known experimentally.”

Even more remarkably, Goldenberg witnessed the emergence of artificial intelligence solutions to the very problem that had driven his research. While structural biology originated with the discovery of X-ray diffraction in the early 20th century, which led to the determination of the first protein structure (myoglobin) in 1958 and the DNA double-helix in 1953, today, programs like AlphaFold can now predict protein structures from amino acid sequences alone — “the definition of the protein folding problem,” as Blair explains.

AlphaFold has predicted the structures of more than a billion proteins, sometimes discovering entirely new folding patterns. Clearly, the field both men have been enmeshed in as researchers, has been transformed by technology. “AlphaFold knows more than we do,” says Blair.

Conscience of the Department

Beyond research, Goldenberg dedicated himself to undergraduate education, serving for years as Associate Director of Undergraduate Programs. Blair describes him as someone who helped “organize the curriculum” and “keep the undergraduates calm to the extent possible” in a large, diverse school serving students with interests ranging from pre-med to research.

“David was … an incredible mentor to me during our work on managing the undergraduate curriculum,” says Naina Phadnis, assistant director of undergraduate programs. “I learned so much from him — he is the most thoughtful and thorough person I have worked with, giving even the smallest tasks careful consideration.” Significantly, Goldenberg navigated undergrad education in biology through the Covid pandemic beginning in 2020.

Earlier, in 2009, Goldenberg received the College of Science Professorship—the award’s inaugural year — for developing an integrated curriculum that bridged traditional separations between chemistry, physics and biology. His course, “Physical Principles of Biology,” reflected both “his intellectual foundations and his taste” and “his belief that we should unify these different parts of the College of Science.”

Blair also remembers Goldenberg as “the conscience of the department” in faculty meetings, “the person who will voice the semi-obvious, uncomfortable issue.” In 2020, Goldenberg joined many prominent scientists in signing a letter to the academic journal Science entitled “Uphold the Nuclear Weapons Test Moratorium,” underscoring his scientific rigor with his signature social conscience.

“I was fortunate to work with David when I began my role as Director of the School of Biological Sciences,” says Fred Adler. “He brought a deep understanding of the working of the University of Utah on par with his understanding of the only slightly less complex topic of nuclear magnetic resonance. With his fierce intelligence and uncompromising moral compass, David had the initially annoying habit of always being right, which I came to appreciate more and more as I learned.”

Stimulating Conversations

The relationship between Blair and Goldenberg, whose labs were located near each other for years, was built on regular lunch conversations that Blair describes as “stimulating.” These discussions often broached fundamental questions about what stabilizes proteins — “memorable” conversations because they concerned “aspects of what stabilizes proteins that are not obvious, not well known.”

Blair recalls Goldenberg sharing insights about the hydrophobic effect, which stabilizes proteins by driving water-avoiding molecules to the protein interior. At higher temperatures relevant to extremophile organisms, this fundamental process actually reverses its physical basis—a discovery that fascinated Goldenberg because “life probably originated and initially evolved at very high temperature.”

“It’s an example of his taste,” explains Blair. “Something that’s really very fundamental, and that is mathematical technical, but its essence is very simple and easy to communicate, and very important.”

Lasting Legacy

As Goldenberg enters retirement, he continues to contribute to the university community. He’s organizing his teaching notes from courses including “Physical Principles of Biology” to make them available online for other instructors, and his richly illustrated book, “Principles of NMR Spectroscopy” published in 2016 continues to have a following among graduate students and advanced undergraduates in the field of chemistry, biochemistry or biology.

For his retirement, Blair had suggested Goldenberg start a microbrewery with a beer named “S = k ln W” — Boltzmann’s fundamental equation for entropy that’s “engraved on Boltzmann’s tomb.”

It’s a fitting tribute to a scientist who found beauty in the mathematical foundations of life itself.

by David Pace