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The joys and vicissitudes of protein science

When invited to look back over a previous life in protein chemistry, I was a little uncertain as to how to proceed but thought that some of my experiences as an author and the inevitable interactions with editors in some of my past research would be appropriate. I believe that scientific discoveries really fall into three categories: first, the serendipity category (“chance to the prepared mind” as Pasteur stated it), of which Roentgen’s finding of X-rays may be the classic example; second, the strategic campaign, somewhat like the deliberate assault on a mountain peak, of which Fred Sangers’s sequencing of insulin might be an example; and third, the solving of the puzzling anomaly, of which the development of the quantum mechanical atom to replace the Bohr atom because atomic spectral details could not be explained by the Bohr atom is an example. My initial interest in enzyme mechanism was influenced importantly by the classic papers of Hans Neurath and Robert Alberty on enzyme kinetics and focused my early work on enzyme mechanism, enzyme kinetics, and protein reagents. I thought a brief account of my experiences in protein chemistry and where they fitted into the categories listed would provide some illumination of the scientific process. I ran into the third category, the “puzzling anomaly” category, in my work on the induced-fit theory. At the time I was a beginning investigator at the Brookhaven National Laboratory and was asked to give a speech at a scientific meeting. As I was preparing the talk about our