Frederic M. Richards pursued undergraduate studies at MIT (B.S.) and graduate studies at Harvard (Ph.D.). Following that, postgraduate work took him from Cambridge, MA to Cambridge, UK via the famous Carlsberg Laboratory in Copenhagen. (For an engaging description, see: F.M. Richards "Linderstrøm-Lang and the Carlsberg Laboratory: the view of a postdoctoral fellow in 1954" Protein Science, 1992, 1: 1721-1730.) Upon completion of postdoctoral work, Fred accepted a faculty position at Yale, where he has remained ever since.
In brief, Fred's scientific contributions – most notably in protein folding – have informed and shaped protein chemistry for approximately half a century. His professional service has been at the very highest levels. And his personal example has inspired several generations of colleagues.
Fred Richards has made fundamental contributions in both experiment and theory. Early in his career (1958), he developed a soon-to-become famous protein system, Ribonuclease S, which was obtained upon limited proteolysis of Ribonuclease A. Surprisingly, the cleaved protein reassociated with exquisite fidelity, retaining biological activity. In Fred's hands, this system became a microcosm for understanding protein molecules – their self-assembly (i.e. folding), activity, energetics, and molecular recognition. With Harold Wyckoff, he used X-ray crystallography to solve the ribonuclease structure, the fourth protein (and second enzyme) to be so elucidated. He demonstrated that the crystal structure is the biologically relevant form, at a time when the issue was still in doubt. Along the way, he made a clever technological innovation to the task of fitting chain to electron density (better known as "Fred's folly").
In contributions to theory, Fred has pioneered the use of surface area and volume to understand protein folding. More than others, this productive approach has been his creation. With B.K. Lee, he devised an early method to calculate surface area, and by himself, applied the Voronoi theorem to determine protein volume. His 1977 review of these topics (F. M. Richards Ann. Rev. Biophys. Bioeng. 1977, 6: 151-176) is a durable masterpiece that spawned a field and, without exaggeration, influenced thousands of working biochemists. Later, with T. Richmond and F. Cohen, this geometric approach was extended to show that excluded volume limits folding to a remarkable degree.
Fred's contributions also include extensive work on other soluble proteins (e.g., thioredoxin), membrane proteins, adiabatic compressibility, chemical probes of accessibility, and algorithm development. The list is long.
Fred Richards has also been a substantial contributor to the National good in professional activities. He served as president of both the American Society of Biochemists and Molecular Biologists and the Biophysical Society and on numerous National councils and editorial boards. Two decades of service to the Jane CoffinChilds Memorial Fund for Medical Research, first as Director and then as board member, identified and launched an all-star cast of younger scientists. His conspicuous wisdom and uncompromising integrity were always in demand for high level planning and/or investigative bodies. Not least, his guidance as Chairman of Molecular Biophysics & Biochemistry at Yale, at a critical moment in the University's history, established MB&B as arguably the foremost department of molecular biophysics in the world at the time.
Fred has been recognized with numerous prestigious awards and has been elected to the most eminent scholarly societies, all the while retaining an irrepressible sense of adventure and just plain fun (admirably captured in: F.M. Richards " Whatever happened to the fun? An autobiographical investigation." Annu. Rev. Biophys. Biomol. Struct., 1997, 26:1-25). On the personal side, he is one of those rare, paradigmatic individuals who make a telling difference in the lives of their colleagues and friends.
-Dr. George Rose, Johns Hopkins University