Sunday, January 25, 2009
Here’s to you, Fred. Your wisdom has been passed to thousands of students. A few of them might match your intellect, but I doubt any of us could measure up. You taught chemistry, biology, sailing, woodworking, engineering, metallurgy, machine shop, engine repair, boat building, epoxy impregnated fiberglass construction, celestial navigation… the list goes on. And all of that was just to me! How long a list would we create if all your students were polled? You taught me subjects which I was explaining to you. Your probing questions and insightful mind made me think deeply about my own field. Your curiosity was infectious. We are all better for having been your students.
What patience you had! To teach teenagers navigation on long sails. To insist we could not leave the dock until everyone could tie a bowline behind their back. To clean up the mess and fix the mistakes as we learned. I am still amazed that you would allow us to take the helm while you slept. Your trust and acceptance of our failures is the example I hold myself to as I teach others what I know. Oh, not that your growl was never heard! You were quick to correct. The snarl of the Captain kept us striving for perfection. But, after the growl came the gruff order to “try again, Laddie”. Your satisfaction when we got it right was the best reward.
You taught me to be prepared. You always had the spare part or the material to make it. The clutter in your shop and garage was the result. In that clutter, you could find the exact piece you remembered saving five years ago. How did you do that? I believe there are enough spare parts on Hekla to rebuild her should she ever break on some remote shore. The boat yard may not understand, but all of us who saw you pull the proper fitting from the bilge learned a lesson.
From you I learned not to fight the storm. The storm will always win. Secure your lines, shorten your sails and wait. The storm will pass and the world will settle down. There is no reason to batter yourself and your boat trying to maintain speed. Have patience, Boyo. Just slow down. You taught it is not failure to heave to for awhile, it is wisdom. I still fight the impulse to push too hard, but when I do, I hear your voice.
Thank you, Fred. I can never repay all you gave me. I can only try to pass to others the lessons you taught. Your storms are behind you. I wish you clear skies, fair winds and deep water. I learn from you still.
In this first picture, Fred was presented with his birthday pancakes in 1997.
Our young son Frank had a stuffed tiger. The parallels with Calvin and Hobbs were unmistakable. We loved the comic strips and found many similarities with life around our house. In 1991, we brought Fred a Calvin and Hobbs book. Fred spent the next hour in tears. I am sure it was sympathy for our situation and not remembrances of George’s (or Fred's) childhood behavior!
In 1997, the gift was a puzzle. This puzzle is created from wooden cubes. Each face of each cube has a different piece of a different picture. So, each piece has 6 sides and 28 possible positions yielding 6 different correct solutions. Fred has just finished calculating the number of possibilities!
Thursday, January 22, 2009
Frederic M. Richards (1925-2009)
Frederic M. Richards, former President of the ASBMB (when it was the American Society of Biological Chemists) and of the Biophysical Society passed away at his home in
Fred Richards was a towering figure in protein chemistry, having played a key role in moving the concept of proteins from amorphous colloids to discrete molecular structures. His contributions to protein science ranged from his central role in founding what is now known as structural biology–both experimental and computational–to the design and application of new chemical reagents for probing protein structure and function.
Richards was born on August 19, 1925, in
In 1963, Richards was appointed Chairman of the Department of Molecular Biology and Biophysics at Yale, which entailed a move from the
Summarizing Richards’ contributions to protein science is difficult, because of the breadth that he covered. A few examples will have to suffice. Much of the early work in Richards’ laboratory focused on bovine pancreatic ribonuclease, and in particular a preparation that he discovered while in Linderstrøm-Lang’s laboratory, dubbed ribonuclease-S (RNaseS) that had been treated with subtilisin, to cleave the peptide bond between Ala20 and Ser21. Richards and coworkers purified and characterized RNaseS, separated it into S-peptide (residues 1-20) and S-protein (residues 21-124), both enzymatically inactive, and showed that S-peptide did not retain an ordered structure in solution but could be reconstituted with S-protein into enzymatically active RNaseS. They crystallized RNaseS and showed that RNaseS was enzymatically active in the crystal, putting to rest the widely held view at that time that protein crystal structures were irrelevant to the conformation and behavior of enzymes in solution. In collaboration with the late H.W. Wyckoff, they solved the structure to atomic resolution (a tie for the third protein structure ever solved to atomic resolution) with and without bound nucleoside monophosphate. While on sabbatical at
The availability of high resolution structures led to the first computational studies (at a time when computational studies required a main frame computer). First were calculations of the accessibility of solvent to the surface of proteins, followed shortly thereafter by calculations of the packing of amino acyl side chains in the interior. These were followed by calculations of the packing of α-helices in myoglobin. Calculations of the interior packing of proteins led much later to calculations of sequences compatible with a particular main chain conformation and in silico protein evolution.
The Richards Lab always included a “wet” component, focused on the properties of proteins in solution and on the design and application of new chemical reagents for modifying proteins in ways that reported on the proteins’ structure and/or function. Types of reagents pioneered in the Richards laboratory included hydrophilic and hydrophobic photoactive reagents for studying membrane protein topology, cleavable cross-linking reagents for studying protein quaternary structure, and reagents that exploited the remarkably strong binding between ferritin and avidin for use in localizing target proteins within cellular structures.
Richards received many honors for his scientific achievements, including the Pfizer-Paul Lewis Award in Enzyme Chemistry (1965), a Guggenheim Fellowship (1967-1968), election as Fellow of the American Academy of Arts and Sciences (1968), election to the National Academy of Sciences (1971), the Kai Linderstrøm-Lang Prize in Protein Chemistry (1978), ASBMB Merck Award (1988), the Stein and Moore Award of the Protein Society (1988), and the State of Connecticut Medal of Science (1995).
What should not be overlooked in reviewing Richards’ science is that the Richards Lab was a wonderful place to develop as a scientist, whether one’s experience there was as an undergraduate student, graduate student, postdoctoral fellow, or sabbatical visitor.
Quotes for use with the Retrospective on Frederic M. Richards
James V. Staros, who had been a graduate student with Fred Richards in the early 1970’s, and who is currently Professor of Biochemistry and Dean of the College of Arts & Sciences at the State University of New York at Stony Brook, remarked, “One of Fred’s outstanding characteristics was his penetrating, almost prescient vision, his ability to see far beyond the experiment at hand. One example: In a paper published in the JBC half a century ago (Richards & Vithayathil  JBC 234: 1459-1465), in which were described the separation of ribonuclease S into enzymatically inactive S-protein and S-peptide and the reconstitution of enzyme activity by the re-association of S-protein and S-peptide, he observed ‘The strength of the interaction in this enzyme system appears to be of the order of magnitude that might be required to explain the initial effects of peptide hormones in the target organs.’ As someone who has spent much of his scientific career working on receptors for one class of polypeptide hormones, I find this remarkably visionary—and typical of Fred.”
Louise Johnson, who spent a postdoctoral year with Fred Richard in 1966 and was a member of the crystallographic team that solved the structure of RNaseS, and who is currently the Sir David Phillips Professor of Molecular Biophysics at
“Fred’s lab was a marvellous place to be. I had also come to learn some biochemistry. Fred was enormously encouraging and was prepared to support some way-out experiments. One such was our attempt to determine the binding site for the platinum heavy atom derivative, platinum diaminodichloride with RNAse, using neutron activation. We travelled by a small plane to Brookhaven where our electrophoresis samples were irradiated. The samples came back red-hot from the sodium in the chromatography paper. Fortunately the activated sodium isotope decayed before the gold isotope of the activated platinum.
We all had tremendous admiration for Fred both for his scientific wisdom, expertise and creativity and also for his extra-science pursuits in ice-hockey and in sailing.
In the following year 1967, Fred and Sally came to
I recall Fred with great affection. He was a marvellous mentor (although I was always a little in awe of him), and great scientist with whom one could discuss a whole range of phenomena (for example diffusion of ligands into proteins and protein crystals), and most of all a person who made science and the life of science great fun.”
Monday, January 19, 2009
Friday, January 16, 2009
New Haven Daily Register:Obituary
Frederic M. Richards died of natural causes at his home in Guilford, CT on January 11, 2009, at the age of 83. He was a Sterling Professor Emeritus of Molecular Biophysics & Biochemistry at Yale University.
Fred was born in New York City in 1925. He graduated from Phillips Exeter Academy in 1944, received a BS in 1948 from the Massachusetts Institute of Technology, and a PhD in 1952 from Harvard University. After completing a postdoctoral program at the Carlsberg Lab in Denmark, he joined the Yale faculty in 1955 and remained there until his retirement in 1991.
During his scientific career, Fred was instrumental in determining the structure of the RNA molecule with Harold Wyckoff. He was the first chair of the Molecular Biophysics and Biochemistry Department at Yale University. He served as a leader in the National Academy of Sciences, and as the scientific director of the Jane Coffin Childs Foundation.
Besides science, Fred Richards had a passion for sailing. He was an active member of the Cruising Club of America, made two trans-Atlantic crossings to England, and many voyages from the coast of Florida to the northern latitudes off Cape Breton, Newfoundland and Labrador.
Fred and his wife, Sally, were active supporters of the Coast Guard Auxiliary, Guilford Land Conservation Trust and its West Woods Trails Committee, and participated in many Faulkner’s Island projects.
He is survived by his wife of 49 years, Sarah (Sally) Wheatland Richards. He also leaves three children: Sarah O. Richards of Coupeville, WA, Ruth G Richards of Cabot, VT, and George H. Richards of Fairfield, CT, and four grandchildren Benjamin H. Lillie of New York City, George H. Richards III, William S. Richards, and Kate E. Richards of Fairfield, CT.
A Memorial Service will be at Yale Battell Chapel on Feb. 12 at 2:00 p.m. with a reception following at New Haven Lawn Club. Memories may be added at any time to the website: fredericmrichards.blogspot.com. In lieu of flowers, donations may be made to Guilford Land Conservation Trust, P.O. Box 200, Guilford, CT 06437 or Woods Hole Oceanographic Institute, Woods Hole, MA 02543.
Thursday, January 15, 2009
Thursday, January 8, 2009
Raghavan Varadarajan aka Rags
Link to photos: http://picasaweb.google.co.in/varadar/Fmr?feat=directlink