Introduction: Murray Goodman's first publication in the chemical literature (published 1953) was primarily physical in nature, not hinting at the breadth and diversity of the 600 or so publications that would eventually express his life's work. This initial offering focused on the incorporation of radiolabelled phosphate into algae under both light and dark conditions. Particularly noteworthy are the subject matter and the principal researcher, Melvin Calvin, Murray's thesis advisor at the University of California at Berkeley. Dr. Calvin was later awarded the Nobel Prize in Chemistry in 1961 for the elucidation of the mechanisms involved in photosynthesis and worked well into his eighties. Murray often said that he would never retire while his years in research were less than those of Melvin.

Murray Goodman, who died on 1 June 2004, was a great peptide scientist with celebrity status, who was showered with awards in his lifetime. Already two Murray Goodman Lectures have been organized [1,2], and several appreciations in memoriam [3-7] have appeared. The University of California at San Diego has established a Murray Goodman Memorial Fund. This special issue of the European Peptide Society's Journal may therefore be thought to call for some explanation. But he was one of its Founding Editors. Further, although he was very much an American, born in Brooklyn on 6 July 1928 and bred there, the influence of his research, teaching, editorial activity and personality was far-reaching in Europe, and his untimely death took place in Europe on one of his frequent trips across the Atlantic. In view of the many commemorations of Murray Goodman which were published soon after his death, and others known to be in the pipeline, we decided to time ours for his first anniversary

Many wonderful comments have been published about Murray Goodman and his science since his untimely passing in June 2004. But working at his side for nearly thirty years gave me insight into this extraordinary man that others—those who only heard him present a lecture or perhaps shared a glass of wine with him at a symposium reception—might have only glimpsed. As I write, I am sitting at the table in the office Murray occupied for so many years at the University of California, San Diego, writing on a yellow pad with a No. 2 pencil as he always did. In putting my thoughts to paper, I thank Lila Gierasch and Charles Deber for inviting me to be Co-Editor of this special Peptide Science issue, and convey a heartfelt thank you to its many contributors.

As a peptide scientist, Murray's interests were broad and eclectic. The name Murray Goodman is synonymous with terms and phrases such as “retro-inverso, Integrated Approach, NCA (N-carboxyanhydride), and TFE (trifluoroethanol),” along with “Do the right thing,” and the still reverberating “What's doing?” Murray began many of his lectures with a slide depicting “The Integrated Approach: Synthesis, NMR, Conformational Analyses, and Biological Assays.” Our goal in preparing this issue was to invite a similarly broad sampling of research by Murray's career-long associates and colleagues, some of whom are publishing for the first time in Peptide Science. Further, we sought to arrange the contributed manuscripts into themes that collectively reflect his integrated approach. As you read this very special issue, I hope you will enjoy the diversity of content these authors have brought to you, and recognize in it the true legacy of Murray's enormous impact....

University professors are supposed to teach, carry out research, and perform professional and community service. For over 50 years, first at Brooklyn Polytech and then at UCSD, Professor Murray Goodman did not simply fulfill each requirement; he excelled at each and every one of them! Not only was Murray an outstanding classroom lecturer, but he also trained over 80 Ph.D's, over 100 postdoctoral students and hosted in his laboratories over 50 visiting scientists from around the world. Just this past spring, his distinguished teaching was applauded with the UCSD Chancellor's Associates Outstanding Teaching Award.

Murray Goodman's research accomplishments and contributions to the fields of organic, polymer, and the biochemistry of peptides and peptidomimetics are formidable and have resulted in over 500 scientific publications. As a leader in his chosen field, Murray also authored textbooks and monographs, led the international peptide society, and served for decades as editor-in-chief of the leading journal in his field, “Biopolymers”. He was a sought after consultant to the chemical and pharmaceutical industries and played key roles in many biotech startups using his peptide chemistry to create new drugs. For his outstanding research and professional service, Murray received numerous awards including the American Chemical Society's Hirschmann, Cope Scholar, and Hermann Mark Awards, just to name a few.

Despite all of his professional commitments, most significantly, Murray Goodman led his community - in fact - all of his communities. For example, he was very involved with the Jewish community and Hillel and served as President of the Beth El Synagogue which he was instrumental in establishing and building in La Jolla.

At UCSD, Murray Goodman mentored younger faculty like ourselves, he led the Organic Chemistry Division, he chaired the Chemistry Department for two terms, and he served as Provost of Revelle College when Paul Saltman became Vice Chancellor. Murray was elected to be Chair of the Faculty Academic Senate and served with distinction, and he helped lead the founding of the Faculty Club which was so critical to creating community at UCSD, and he served as its president.

The untimely death of Professor Murray Goodman of the University of California, San Diego on June 1, 2004 after a short but severe illness was a great shock and left a gaping hole in Peptide Science and in Chemistry. Murray was one of the founders and leading lights in modern peptide chemistry. His scientific work covered the full range of peptide science from the synthetic and mechanistic aspects of peptide and peptidomimetic synthesis, to structural and conformational methods, to structure-biological activity relationships, to computational chemistry and biophysical studies. All were integral parts of Murray's view of peptide science, and of its central role in modern chemistry and biology. His many seminal contributions to peptide science and to nurturing young (and older) peptide scientists worldwide are a lasting legacy. It is a great honor and privilege to dedicate this and the next issue of The Journal of Peptide Research to the memory of Murray Goodman. My sincere thanks to everyone who has contributed to these issues. I am sure that Murray's family, and his many friends and colleagues, will be very pleased.

Murray's career has been long and distinguished. He received his B.S. from Brooklyn College and went west for his Ph.D. at the University of California, Berkeley, working with Nobel Laureate Melvin Calvin. He then did his postdoctoral work at MIT in Boston and at Cambridge University in England, before beginning his independent academic career at the Polytechnic Institute of Brooklyn in 1956. In 1964, he became a Full Professor there, and in 1967 the Director of the Polymer Research Institute. The lure of the west and the excellence of the University of California, San Diego drew him there in 1970 as a Professor of Chemistry where he remained throughout the rest of his career, serving as Chairman of the Department of Chemistry from 1978 to 1982 and as Acting Provost at Revelle College from 1972 to 1974. He was revered as an outstanding teacher and mentor. About 80 young scientists received their Ph.D. under Murray's guidance and he also mentored more than 200 postdoctoral fellows. Many of these students and associates have since gone on to outstanding careers of their own in academia and industry. For his excellence in these areas, Murray received the UCSD Chancellor's Associates Recognition Award for Excellence in Graduate Teaching, and very recently the endowment of the Goodman Chair in Chemistry at UCSD...

Murray Goodman was an engaging colleague, a great scientist, and above all, a good friend to the many people that knew him. I was one of those fortunate people who knew Murray well and considered him to be my friend. Indeed, Murray was instrumental in bringing me to La Jolla to join UCSD and Scripps in 1989 and for that I will be forever grateful to him. His influence on my career did not stop there, for he was always loyal to me as a colleague and friend. I remember with fondness the frequent telephone calls I received from him whether it was to talk about some issue in the department or some news he wanted to share with me, or simply to invite me to lunch for companionship and discussion.

Murray was also my neighbor in La Jolla Farms, a community in which he took great pride and enriched through many initiatives. We would always meet at parties of the community and share delicious ethnic foods, ideas, concerns and future plans. With Zelda by his side, they would always seek out Georgette and me for a chat or to invite us to dinner at their house, and through these encounters we came to appreciate both their warmth and concern for their neighbors and fellow citizens.

As a scientist, Murray Goodman was respected around the world, his name being almost synonymous with peptide chemistry. Indeed, when it came to combining molecular design, synthesis and biological evaluation of peptides and peptide mimetics, Murray was the best, simply the master. I remembered the pride and content with which he would present me as a gift each and every volume of the Houben-Weyl series on peptides, which he edited, as they were published. He took pride in his work and his students. His energy was unparalleled and his enthusiasm infectious. Murray simply loved his science and he devoted an enormous amount of his strength to it - teaching, researching, motivating, and inspiring. He was literally everywhere, doing everything that had to be done, whether it was in the department, at home, or in the community. He was also loved and admired internationally. Indeed, I have not been to a country where his name was not mentioned with affection by those who considered him as a pioneer, a bundle of energy and a good friend.

Murray Goodman will be remembered for his warmth as much as for his science and engaging personality. His countless friends and admirers will always hold him dear to their hearts. The photo below shows him among some of his friends and colleagues attending a recent Symposium at The Scripps Research Institute, a habit he always had time for.

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ly active poly(d-β-phenylpropyl isocyanate) has been synthesized. The optically active polymer has a negative optical rotation, opposite in sign to that of the monomer and of the model compound, but of greater magnitude. This enhanced optical activity shows that the polymer probably assumes a preferred conformation. A comparative circular dichroism (CD) study of this polymer and of a model compound indi- cates that dissymmetry in the polymer backbone and the aromatic side chains contribute to the CD spectrum of the optically active polymer. The nuclear magnetic resonance spectrum of the optically inactive polymer shows broad absorption bands while the spectrum of the optically active polymer has sharp peaks. This is consistent with our assumption that the optically active polymer possesses a preferred conformation, The optically active poly- mer is insoluble in most organic solvents. Chloroform represents a notable exception which may arise from a specific interaction between this solvent and the urea-like nature of the main chain.

The synthesis of four enkephalinamide analogs is described in which the peptide bond between residues 4 and 5 is reversed with or without simultaneous reversal of the carboxyl-terminal amide bond.These so-called partially modified retro-inverso-isomers are new, potent, topochemical analogs of the enkephalines.Tests, both in vitro and in vivo, have shown that these analogs are considerably longer acting than any previously studied enkephalins.Thus, partial reversal of the peptide bonds of the backbone can result in peptides with enhanced activity compared to a parent compound, provided that the structural complementary of both the side chains and end groups are conserved.

We studied the conformation of a series of γ-ethyl-L-glutamate oligopeptides by circular dichroism and 220 MHz nuclear magnetic resonance spectroscopy. By use of the first technique we noted enhancement of the n→0 π*and splitting of the ir π→πr* transitions commencing with the heptamer in trimethylphosphate and trifluoroethanol. With the second method we found changes in chemical shifts for the amide protons consistent with the onset of helicity at the heptamer in the solvents noted above. When DMSO-d6 is used as a solvent, no such chemical shift changes occur because the oligopeptides do not assume helical conformations.

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