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Elegant Molecules: [Dr. Stanford Moore] Fulvio Bardossi Rockefeller University Digital Commons @ RU Rockefeller University Research Profiles Campus Publications Spring 1982 Elegant Molecules: [Dr. Stanford Moore] Fulvio Bardossi Judith N. Schwartz Follow this and additional works at: http://digitalcommons.rockefeller.edu/research_profiles Part of the Life Sciences Commons Recommended Citation Bardossi, Fulvio and Schwartz, Judith N., "Elegant Molecules: [Dr. Stanford Moore]" (1982). Rockefeller University Research Profiles. Book 13. http://digitalcommons.rockefeller.edu/research_profiles/13 This Article is brought to you for free and open access by the Campus Publications at Digital Commons @ RU. It has been accepted for inclusion in Rockefeller University Research Profiles by an authorized administrator of Digital Commons @ RU. For more information, please contact [email protected]. Carbo I Leu ------Asn--------.....) THE ROCKEFELLER UNIVERSITY I 18 _ C,.---------~~----.-- ....---_...980....101_------~ His (P'o) ~-----------His--- ...../IIB RESEARCH 131 170 s 5 Diagram ofspecial pllDOIi\1CIIES features ofbovine 206 N J.L pancreatic deoxyribonuclease. ......------------Thr SPRING 1982 257 Elegant Molecules Asked how he happened to become a biochemist, Professor FROM THE GREEKPROTEIOS: Stanford Moore attributes the choice to gifted teachers of PRIMARY science and a vocational counselor who advised him that there was no future in aeronautical engineering. "But," he adds Proteins comprise the largest part of the solid mattel ofliving with a smile, ''I've never regretted the choice. I can imagine cells. Some proteins, such as the hemoglobin that carries oxy­ no life more fascinating or more rewarding than one spent gen in red blood cells, are involved in transport and stOrage. exploring the elegant and complicated architecture of organic Many hormones, like insulin, are proteins; they are chemical molecules." messengers that coordinate body activities. Immunoglobu­ In 1963, Dr. Moore and his Rockefeller University col­ lins, the master molecules of immunity, are proteins. (In the league, William H. Stein, reported that their laboratory had same year that Dr. Moore and Dr. Stein received their Nobel determined the chemical structure of the first enzyme and Prize, Professor Gerald M. Edelman ofThe Rockefeller Uni­ largest protein to be decoded up to that time: pancreatic versity shared the Nobel Prize in Physiology or Medicine for ribonuclease. In 1972, Dr. Moore and Dr. Stein shared the determining the chemical structure of an immunoglobulin, Nobel Prize in Chemistry with Christian B. Anfinsen of the work facilitated by technology refined in the Moore-Stein National Institutes of Health for their contributions to the laboratOry.) All known enzymes are proteins. Enzymes, thou­ understanding of the interrelationships of the structure and sands of them, are the catalysts of innumerable body pro­ activity of the ribonuclease molecule. cesses. They can speed the rates of chemical reactions more Dr. Stein died in 1980. At his memorial service, the late than a millionfold. Philip Handler, then president of the National Academy of Chemically speaking, proteins are large-they are termed Stanford Moore Sciences, characterized the 40-year Moore-Stein partnership . macromolecules. There are proteins with molecular weights as "surely among the most productive cooperative endeavors that exceed 100,000 (based upon the weight of a hydrogen in the histOry ofscience." atOm as 1). Proteins are constructed primarily from smaller The research continues today under Dr. Moore's molecules, about 20 kinds in all, called amino acids. Two or leadership. more amino acids linked tOgether form what is called a pep- Pa~~ 2 tide. A protein is a very large, structurally complex polypep­ World War II, during which time the group worked with the tide chain. Some smaller peptides, like their larger relatives, Office of Scientific Research and Development investigating also handle important jobs. One of the most heralded events properties of chemical warfare agents. Dr. Moore, sent to in the neurosciences in recent y~ars was the discovery of Washington to facilitate liaison between science and the mili­ endorphins, natural opiates in the brain. The endorphins are tary, wound up with the Operational Research Section in the peptides. Pacific theater. At the war's end, Dr. Moore and Dr. Stein Not surprisingly, when something goes wrong with the resumed their collaboration, now with a laboratory of their body's protein chemistry, trouble can follow. There are more own, eager to explore some "interesting developments" that than 100 hereditary diseases known to involve specific pro­ had occurred in the interim, particularly in the field of tein defects. Parkinson's disease and phenylketonuria (PKU), chromatography. which can lead to mental retardation, result from enzyme deficiencies. The replacement of one specific amino acid by another in one of the polypeptide chains of the hemoglobin SEPARATING THINGS molecule results in sickle-cell anemia. Scientists use a variety of techniques to separate, identify, and Joshua Lederberg, president of The Rockefeller Univer­ purify chemical compounds. One of those techniques, chro­ sity, recently wrote: "Almost everything we attempt in matography, was introduced early in the century by a Russian rational medicine is connected with the structure and behav­ botanist, Michael Tswett. In his original procedure, a petro­ ior of proteins. Our hopes for radical interventions to prevent leum ether extract of green leaves was poured into a glass or reverse such complex processes as cancer or aging can tube packed wit~ calcium carbonate and clear solvent was scarcely outpace that knowledge." added. The leaf pigments, adhering differently to the calcium In 1939, when Stanford Moore arrived at what was then carbonate because oftheir various molecular characters, sepa­ The Rockefeller Institute for Medical Research, very little rated into bands of different colors as they moved down the was known of detailed protein structure. Recommended by column. The bands could then be washed OUt of the column, his professor at the University of Wisconsin, he had been color by color. Tswett's column was later adapted for color­ invited to join the laboratory of Max Bergmann, to which less compounds through the use of specific methods of detec­ another recent Ph.D. in biochemistry, William Stein, had tion and visualization. come two years earlier. Bergmann was working on techniques Chromatography emerged as a major tool of biochemical for separating individual amino acids from hydrolysates of science after 1941, when English researchers A.]. P. Martin Stanford Moore in the proteins. He assigned his two juniors the task of developing and R.L.M. Synge introduced what they called partition chro­ laboratory. ways for determining the precise quantities of each of the matography, which made it practical to separate water-soluble amino acids from which a protein is built. compounds such as amino acids and peptides. Drs. Stein and "Dr. Bergmann's goal," says Dr. Moore, "was to find out­ Moore, among others, appreciated the potential of partition because we really didn't know then-whether proteins actu­ chromatography for the quantitative separation of amino ally had specific structures. Could we write a formula for acids. Following a suggestion by Dr. Synge, they began by them? To do that, we had to find out precisely what they were using a column of moist potato starch with organic solvents. made of." When a mixture of amino acids was passed through the starch Bergmann, who died in 1944, never saw the full realization column, and fractions (each composed of a given number of of his goal. The laboratory's research on protein structure had drops) were collected, the amino acids were washed off been suspended with the entry of the United States into serially. Thus began a period of innovation and invention- Page 3 the "tooling up," as Dr. Moore has called it-that has had far­ 0.3 reaching effects on laboratory technology. Jl1 reonine Glutamic acid The amino acids in an acid The starch chromatogram was, indeed, a great improve­ Aspartic hydrolysate 0/ ribonuclease A, acid ~ / Sepine ment over earlier methods of separation. The drop collecting, / Alanine determined manually by however, as Dr. Moore recalls, was "a tedious and time-con­ I ion-exchange chromatography suming process, and I, as the bachelor, always got the night ~ (1954). shift. Bill and I decided that some simple automation would Proline be desirable." Drawing upon the skills of The Rockefeller Institute's instrument makers, they fashioned an automatic ,.... Glycine fraction collector, which, unattended, could collect and count , A fractions, moving from tube to tube. (The photoelectric eye that they used was adapted from one originally designed to center the transparent wrappers on packages of chewing w A gum.) About this time the laboratory also made quantitative Effluent m1.150 zoo 250 300 I- 30° .1 • 50°------ the use of ninhydrin, a reagent that yields a blue color, for ,- Influent 0.2N pH 3.1-----·~1.....- estimating the extremely small amounts of amino acid in each 0.2 -------------------- of the fractions. The intensity of the color given to a fraction Cystine /Methionine by the reagent is proportional to the amount of amino acid VQ1in~~me50 rr '/I501eucine TyP05ine that it contains. 0.1 - ) /Leucine For a number of years, Dr. Moore and Dr. Stein and their /Pl1enyl­ ~. group searched for a better adsorbent than starch. They alanine found
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