1963: Synthesis and Structure of Macromolecules, Vol. XXVIII
Organizer: H. Edwin Umbarger
Foreword v
List of Previous Volumes vii
Photographs of Some Symposium Participants viil
List of Those Attending the Symposium x
Francis J. Ryan xx THE SYNTHESIS AND STRUCTURE OF DNA RIS, H. and B. L. CHANDLER. The Ultrastructure of Genetic Systems in Prokaryotes and Eukaryotes RICHARDSON, C. C., C. L. SCHILDKRAUT and A. KORNBERG. Studies on the Replication of DNA by DNA Polymerases 9 BOLLUM, F. J. Studies on the Nature of Calf Thymus DNA-Polymerase Products 21 BURTON, K., M. R. LUNT, G. B. PETERSEN, and J. C. SIEBKE. Studies of Nucleotide Sequences in DNA 27 MOSIG, G. Genetic Recombination in Bacteriophage T4 During Replication of DNA Fragments 35 CAIRNS, J. The Chromosome of Escherichia coli 43 SUEOKA, N., and H. YOSHIKAWA. Regulation of Chromosome Replication in Bacillus subtilis 4. 47 NAGATA, T. The Sequential Replication of E. coli DNA 55 THE SYNTHESIS AND STRUCTURE OF RNA HURWITZ, J., A. EVANS, C. BABINET, and A. SKALKA. On the Copying of DNA in the RNA Polymerase Reaction 59 CHAMBERLIN, M., and P. BERG. Studies on DNA Directed RNA Polymerase; Formation of DNA-RNA Complexes with Single Stranded f X 174 DNA as Template 67 SPENCER, M. X-Ray Diffraction Studies of the Secondary Structure of RNA 77 FRESCO, J. R., L. C. KLOTZ, and E. G. RICHARDS. A new Spectroscopic Approach to the Determination of Helical Secondary Structure in Ribonucleic Acid 83 HASELKORN, R. Actinomycin D as a Probe for Nucleic Acid Secondary Structure 91 AUGUST, J. T., S. COOPER, L. SHAPIRO, and N. D. ZINDER. RNA Phage Induced RNA Polymerase 95 WEISSMANN, C., L. SIMON, P. BORST, and S. OCHOA. Induction of RNA Synthetase in E. coli After Infection by the RNA Phage, MS 2 99 BALTIMORE, D., and R. M. FRANKLIN. Properties of the Mengovirus and Poliovirus RNA Polymerases l" 105 SPIEGELMAN, S., and R. H. Dol. Replication and Translation of RNA Genomes 109 TRANSFER RNA HOLLEY, R. W., J. APGAR, G. A. EVERETT, J. T. MADISON, S. H. MERRILL, and A. ZAMIR. Chemistry of Amino Acid-Specific Ribonucleic Acids 117 CANTONI, G. L., H. ISHIKURA, H. H. RICHARDS, and K. TANAKA. Studies on Soluble Ribonucleic Acid. XI. A Model for the Base Sequence of Serine S-RNA `% 123 INGRAM, V. M. and J. A. SJOQUIST. Studies on the Structure of Purified Alanine and Valine Transfer RNA from Yeast 133 BOREK, E. The Methylation of Transfer RNA: Mechanism and Function 139 GOLD, M., and J. HURWITZ. The Enzymatic Methylation of the Nucleic Acids 149 LITTAUER, U. Z., K. MUENCH, P. BERG, W. GILBERT, and P. F. SPAHR. Studies on Methylated Bases in Transfer RNA 157 MESSENGER RNA SPIEGELMAN, S., and M. HAYASHI. The Present Status of the Transfer of Genetic Information and Its Control 161 LEVINTHAL, C., D. P. FAN, A. RIGA, and R. A. ZIMMERMAN. The Decay and Protection of Messenger RNA in Bacteria MARMUR, J., C. M. GREENSPAN, E. PALECEK, F. M. KAHAN, J. LEVINE, and M. MANDEL. Specificity of the Complementary RNA formed by B. subtilis Infected with Bacteriophage SP8 191 HALL, B. D., M. H. GREEN, A. P. NYGAARD, and J. A. BOEZI. Copying of DNA in T2 Infected E.coli 201 BAUTZ, E. K. F. The Structure of T4 Messenger RNA in Relation to Messenger Function 205 DARNELL, J. E., S. PENMAN, K. SCHERRER, and Y. BECKER. A Description of Various Classes of RNA from Hela Cells 183 PROTEIN SYNTHESIS I HARDESTY, B., R. ARLINGHAUS, J. SHAEFFER, and R. SCHWEET. Hemoglobin and Polyphenylanine Synthesis with Reticulocyte Ribosomes. 215 MARKS, P. A., E. R. BURKA, R. RIFKIND, and D. DANON. Polyribosomes Active in Reticulocyte Protein Synthesis 223 NAKAMOTO, T., T. W. CONWAY, J. E. ALLENDE, G. J. SPYRIDES, and F. LIPMANN. Formation of Peptide Bonds I. Peptide Formation from Aminoacyl-S-RNA 227 BENNETT, T. P., J. GOLDSTEIN, and F. LIPMANN. Formation of Peptide Bonds II. Coding Properties of Leucyl-S-RNAs 233 WOOD, W. B., and P. BERG. Studies on the "Messenger" Activity of RNA Synthesized with RNA Polymerase 237 ALLFREY, V. G., and A. E. MIRSKY. Mechanisms of Synthesis and Control of Protein and Ribonucleic Acid Synthesis in the Cell Nucleus 247 MACH, B. The Biosynthesis of an Antibiotic Polypeptide, as Distinguished from Protein Biosynthesis 263 SPIRIN, A. S. In Vitro Formation of Ribosome-like Particles from CM Particles and Protein 267
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PROTEIN SYNTHESIS II RICH, A., J. R. WARNER, and H. M. GOODMAN. The Structure and Function of Polyribosomes 269 GILBERT,W.Protein Synthesis in E.coli 287 GROS, F., J. M. DUBERT, A. TISSIERES, S. BOURGEOIS, M. MICHELSON, R. SOFFER, and L. LEGAULT. Regulation of Metabolic Breakdown and Synthesis of Messenger RNA in Bacteria 299 NOMURA,M.Mode of Action of Colicines 315 KEPES, A. Kinetic Analysis of the Early Events in Induced Enzyme Synthesis 325 REGULATION OF SYNTHESIS OF MACROMOLECULES JACOB, F., S. BRENNER, and F. CUZIN. On the Regulation of DNA Replication in Bacteria 329 AMES,B.N.,andP.E.HARTMAN.The Histidine Operon 349 MARTIN, R. G. The One Operon-One Messenger Theory of Transcription 357 ATTARDI, G., S. NAONO, J. ROUVIERE, F. JACOB, and F. GROS. Production of Messenger RNA and Regulation of Protein Synthesis 363 GUTTMAN, B., and A. NOVICK. A Messenger RNA for b-Galactosidase in E. coli 373 EPSTEIN, R. H., A. BOLLE, C. M. STEINBERG, E. KELLENBERGER, E. BOY, DE LA TOUR, R. CHEVALLEY, R. S. EDGAR, M. SUSMAN, G. DENHARDT, and A. LEILAUSIS. Physiological Studies of Conditional Lethal Mutations of Bacteriophage T4 D 375 THOMAS, C. A. The Arrangements of Nucleotide Sequences in T2 and T5 DNA Molecules 395 N0VICK, A., E. S. LENNOX, and F. JACOB. Relationship Between Rate of Enzyme Synthesis and Repressor Level 397 REVEL, H., and S. E. LURIA. On the Mechanism of Unrepressed Galactosidase Synthesis Controlled by a Transducing Phage 403 SCHACHMAN, H. K. Considerations on the Tertiary Structure of Proteins 409 ZABIN, I.Proteins of the Lactose System 431 BACON, D., and H. J. VOGEL. A Regulatory Gene Simultaneously Involved in Repression and Induction 437 TERTIARY STRUCTURE OF PROTEINS EPSTEIN, C. J., R. F. GOLDBERGER, and C. B. ANFINSEN. Genetic Control of Tertiary Protein Structure: Studies with Model Systems 439 MUIRHEAD, H., and M. F. PERUTZ. Structure of Reduced Human Hemoglobin 451 ALLOSTERIC INTERACTIONS BETWEEN PROTEINS AND SMALL MOLECULES TOMKINS, G. M., K. L. YIELDING, N. TALAL, andJ. F. CURRAN. Protein Structure and Biological Regulation 461KOSHLAND, D. E., JR. The Role of Flexibility in Enzyme Action 473 WYMAN, J. Allosteric Effects in Hemoglobin 483 GERHART, J. C., and A. B. PARDEE. The Effect of the Feedback Inhibitor, CTP, on Subunit Interactions in Aspartate Transcarbamylase 491 CHANGEUX, J. P. Allosteric Interactions on Biosynthetic L-Threonine Deaminase from E.coli K-12 497FREUNDLICH, M., and H. E. UMBARGER. The Effects of Analogues of Threonine and of Isoleucine on the Properties of Threonine Deaminase 505 COHEN, G. N., and J. C. PATTE. Some Aspects of the Regulation of Amino Acid Biosynthesis in a Branched Pathway 513 COMPLEMENTATION FINCHAM, J. R. S., and A. CODDINGTON. The Mechanism of Complementation between am Mutants of Neurospora crassa 517 PERRIN, D. Complementation between Products of the beta-Galactosidase Structural Gene of E. coli 529 ZIPSER, D., and D. PERRIN. Complementation on Ribosomes 533 SCHLESINGER, M. J., A. TORRIANI, and C. LEVINTHAL. In Vitro Formation of Enzymatically Active Hybrid Proteins from E. coli Alkaline Phosphatase CRM's 539 GROSS, S. R., and R. E. WEBSTER. Some Aspects of Interallelic Complementation Involving Leucine Biosynthetic Enzymes of Neurospora 543 AMINO ACID CODE I: EVIDENCE FROM IN VITRO SYSTEMS NIRENBERG, M. W., O. W. JONES, P. LEDER, B. F. C. CLARK, W. S. SLY, and S. PESTKA. On the Coding of Genetic Information 549 PEYER, J. F., P. LENGYEL, C. BASILIO, A. J. WAHBA, R. S. GARDNER, and S. OCHOA. Synthetic Polynucleotides and the Amino Acid Code 559 YAMANE, T., T. Y. CHENG, and N. SUEOKA. Species Specificity of Amino Acid Transfer-RNA and Amino Acyl-T-RNA Synthetase 569 WEINSTEIN, I. B. Comparative Studies on the Genetic Code 579 AMINO ACID CODE II: EVIDENCE FROM AMINO ACID SUBSTITUTIONS YANOFSKY , C. Amino Acid Replacements Associated with Mutation and Recombination in the A Gene and Their Relationship to In Vitro Coding Data 581 WITTMANN, H. G., and B. WITTMANN-LIEBOLD. Tobacco Mosaic Virus Mutants and the Genetic Coding Problem 589 FRANCIS J. RYAN Centers of scientific research are what people choose to make them. This is especially true for the Laboratory at Cold Spring Harbor, which has achieved its scientific reputation not by some happy accident but as the result of the careful guidance of its loyal friends. A few of these friends have at some time worked here for long periods. Others have been regular summer visitors. And others, though never here for very long, have yet shown themselves ready to forsake their own affairs on behalf of the Laboratory in times of need.
This last year saw the withdrawal of the Carnegie Institution of Washington from Cold Spring Harbor and the creation of anew organization "The Cold Spring Harbor Laboratory of Quantitative Biology" to control the entire enterprise. Many people have labored to make the transition possible and so ensure the continued survival of the laboratories. No one worked harder at this than Francis Ryan.
Despite his responsibilities as Chairman of the Department of Zoology at Columbia University, he joined with Dr. Edward L. Tatum and Dr. Rollin D. Hotchkiss in carrying out the early negotiations with the Long Island Biological Association and the Carnegie Institution. Later he became one of the most active of the group of Trustees formed to watch over the new Laboratory at Cold Spring Harbor. In this role, he was ready at all times to give his selfless support and counsel, and to exercise his great powers of gentle persuasion.
Francis Ryan died suddenly, one month after the end of this symposium.The news of his death had the unbelievable quality that comes with the death of a friend. Time will soften this blow, but it will not lessen the great contribution he made to science-through his own research, through the work he inspired in others, and through his great influence on the course of events during a most critical period in the affairs of the laboratory at Cold Spring Harbor. He was 47 at the time of his death.
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