A remembrance of Elkan R. Blout

As a medical student at Harvard Medical School, Lubert Stryer carried out research in Elkan Blout's laboratory. He delivered the following remembrance at the Memorial Service for Elkan Blout on January 26, 2007 at Harvard Memorial Church.

I first met Elkan in the autumn of 1957, a few weeks after entering Harvard Medical School. I was eager to carry out part-time research in combination with my medical studies, and contacted Dr. Sidney Farber, the Director of the Children's Cancer Research Foundation, in the hope I could find an opening there. He suggested that I see an unusual scientist, a Dr. Elkan R. Blout, who was Director of Chemical Research at Polaroid by day and head of a basic research laboratory at Children's Hospital by night. That evening, I met Elkan and was immediately captivated by his breadth, energy, and vision. He told me about his research on synthetic polypeptides as models of proteins, and showed me around his lab, which was really humming. At the end of the evening, I was thrilled when Elkan offered me a research position. That was the beginning of nearly 50 years of a wonderful association that profoundly transformed and enriched my life.

Elkan's research was centered on a fundamental question: What is the relationship between the amino acid sequence of proteins and their three-dimensional structures? Proteins are constructed from a repertoire of 20 amino acids. The chains of amino acids fold into intricate three-dimensional forms that enable proteins to carry out an exceptionally wide range of functions, such as enzymatic catalysis, coordinated motion, mechanical support, immune protection, and the transmission of nerve impulses. Elkan's approach to this daunting problem was to synthesize synthetic polypeptides—initially, long chains of a single kind of building block—and then learn about their conformation, their three-dimensional structure, by using light. Elkan brought together synthetic organic chemistry and spectroscopy to create a new field that illuminated our understanding of how protein architecture is specified.

In 1960, Elkan, together with Christiane de Lozé, Stan Bloom, and Gerry Fasman, published an incisive and seminal paper in the Journal of the American Chemical Society entitled “The Dependence of the Conformations of Synthetic Polypeptides on Amino Acid Composition.” They discovered that some amino acids lead to an α-helix, others to a β-sheet, and others to a random coil, and explained why. They concluded:

“It seems probable that the effects described here on the relationship between amino acid composition and polypeptide structure also are operative in protein structures. When a sequence of β or random-forming amino acids is contiguous to an α-helical section of a protein chain this may be a site where a loop or reversal of direction can occur.”

Exactly right. This seminal research was a fundamental breakthrough in understanding why nature selected an alphabet of 20 amino acids and how this repertoire is used to shape the form of proteins.

Elkan was a superb mentor. He helped his students and fellows choose important research problems that were experimentally accessible with the latest technologies. He provided just the right degree of guidance in the course of the research. Elkan worked closely and tirelessly with the people in his lab in writing manuscripts and preparing research talks—he highly valued effective communication. He was also deeply concerned about the research careers of his students and fellows. He thought about what each needed at the next stage and opened the doors of opportunity. In my fourth year of medical school, Elkan sent me upstairs to Carolyn Cohen's lab to learn X-ray diffraction because he felt that my experimental background should be broadened. When I decided to pursue basic research rather than an internship, Elkan told me that he had arranged for me to move across the river to Ed Purcell so that I would learn some physics, and then to John Kendrew in Cambridge, England, to work on X-ray crystallography. Students today often apply to a large number of laboratories for a postdoctoral position and then agonize over where to go next. For me, it was very simple—Elkan gave me my marching orders, which I gratefully accepted.

Elkan's students and postdocs, and the alumni of his lab, benefited in yet another way. Many outstanding scientists from around the world have visited his lab, some for extended periods. We were introduced to highly creative and vibrant scientists such as Ephraim Katchalski-Katzir, Yuri Ovchinnikov, Nelson Leonard, and Jean-Marie Lehn. They greatly valued Elkan and cherished his friendship. And we in turn were welcomed to their laboratories and enjoyed their scientific fellowship and hospitality. Let me add that Elkan was always there helping when his friends or his scientific family were struck by adversity.

Elkan did so much to enhance and strengthen the scientific and educational life of the nation as Chairman of the Department of Biological Chemistry at Harvard Medical School, Dean for Academic Affairs at its School of Public Health, Treasurer of the National Academy of Sciences and the American Academy of Arts and Sciences, and Senior Adviser to the Food and Drug Administration. His exemplary service and leadership over many decades has been inspiring. He was always a voice of reason, civility, and wisdom.

We are deeply grateful to Elkan for his enduring contributions to science, his sustained nurturing of students and institutions, his generosity of spirit, and his devoted friendship. How very fortunate for all of us! What a remarkable and wonderful legacy for the four generations of his family!