Electron Microscopy: J. Frank, M. Radermacher, T. Wagenknecht, and A. Verschoor, Studying Ribosome Structure by Electron Microscopy and Computer-Image Processing. G. Harauz, E. Boekema, and M. van Heel, Statistical Image Analysis of Electron Micrographs of Ribosomal Subunits. M. Boublik, G.T. Oostergetel, V. Mandiyan, J.F. Hainfeld, and J.S. Wall, Structural Analysis of Ribosomes by Scanning Transmission Electron Microscopy. G. Stvffler, B. Redl, J. Walleczek, and M. Stvffler-Meilicke, Identification of Protein-Protein Cross-Links within the Escherichia coli Ribosome by Immunoblotting Techniques. I.N. Shatsky and V.D. Vasiliev, Electron Microscopy Studies of Ribosomal RNA. Other Biophysical Methods: A. Yonath and H.G. Wittmann, Crystallographic and Image Reconstruction Studies on Ribosomal Particles from Bacterial Sources. M.S. Capel and V. Ramakrishnan, Neutron-Scattering Topography of Proteins of the Small Ribosomal Subunit. P. Nowotny, V. Nowotny, H. Voss, and K.H. Nierhaus, Preparation and Activity Measurements of Deuterated 50S Subunits for Neutron-Scattering Analysis. V.N. Bushuev and A.T. Gudkov, Nuclear Magnetic Resonance Techniques for Studying Structure and Function of Ribosomes. P.B. Moore, S. Abo, B. Freeborn, D.T. Gewirth, N.B. Leontis, and G. Sun, Preparation of 5S RNA-Related Materials for Nuclear Magnetic Resonance and Crystallography Studies. O.W. Odom, H.-Y. Deng, and B. Hardesty, Fluorescence Labeling and Isolation of Labeled RNA and Ribosomal Proteins. P.H. van Knippenberg and H.A. Heus, Isolation and Characterization of Colicin Fragments of Bacterial 16S Ribosomal RNA. Protein-RNA Interactions: D.E. Draper, I.C. Deckman, and J.V. Vartikar, Physical Studies of Ribosomal-Protein-RNA Interactions. D.E. Draper, S.A. White, and J.M. Kean, Preparation of Specific Ribosomal RNA Fragments. E. Wickstrom and L.G. Laing, Physical Studies of the Interaction of Escherichia coli Translational Initiation Factor 3 Protein with Ribosomal RNA. L.-M. Changchien, R. Conrad, and G.R. Craven, Isolation of Fragments of Ribosomal Proteins That Recognize rRNA. D.B. Datta, L.-M. Changchien, and G.R. Craven, Isolation of Kinetic Intermediates in in Vitro Assembly of the Escherichia coli Ribosome Using Cibacron Blue F3GA. R. Lietzke and K.H. Nierhaus, Total Reconstitution of 70S Ribosomes from Escherichia coli. Cross-Linking and Affinity-Labeling Methods: R. Brimacombe, W. Stiege, A. Kyriatsoulis, and P. Maly, Intra-RNA and RNA-Protein Cross-Linking Techniques in Escherichia coli Ribosomes. A. Expert-Bezangon and C. Chiaruttini, RNA-Protein Cross-Linking. P.L. Wollenzien, Isolation and Identification of RNA Cross-Links. S.E. Lipson and J.E. Hearst, Psoralen Cross-Linking of Ribosomal RNA. B.S. Cooperman, Affinity Labeling of Ribosomes. E. Kuechler, G. Steiner, and A. Barta, Photoaffinity Labeling of Peptidyltransferase. J. Ofengand, R. Denman, K. Nurse, A. Liebman, D. Malarek, A. Focella, and G. Zenchoff, Affinity Labeling of tRNA-Binding Sites on Ribosomes. Chemical and Enzymatic Probing Methods: W.E. Hill, D.G. Camp, W.E. Tapprich, and A. Tassanakajohn, Probing Ribosome Structure and Function Using Short Oligodeoxyribonucleotides. D. Hartz, D.S. McPheeters, R. Traut, and L. Gold, Extension Inhibition Analysis of Translation Initiation Complexes. M.M. Yusupov and A.S. Spirin, Hot Tritium Bombardment Technique for Ribosome Surface Topography. A.A. Bogdanov, N.V. Chichkova, A.M. Kopylov, A.S. Mankin, and E.A. Skripkin, Surface Topography of Ribosomal RNA. J. Christiansen and R. Garrett, Enzymatic and Chemical Probing of Ribosomal RNA-Protein Interactions. P.W. Huber and I.G. Wool, Use of ~ga-Sarcin to Analyze Ribosomal RNA-Protein Interactions. B.J. Van Stolk and H.F. Noller, Use of RNA-DNA Hybridization in Chemical Probing of Large RNA Molecules. S. Stern, D. Moazed, and H.F. Noller, Structural Analysis of RNA Using Chemical and Enzymatic Probing Monitored by Primer Extension. Immunological Methods: D.G. Glitz, P.A. Cann, L.S. Lasater, and H.M. Olson, Antibody Probes of Ribosomal RNA. M. Stvffler-Meilicke and G. Stvffler, Localization of Ribosomal Proteins on the Surface of Ribosomal Subunits from Escherichia coli Using Immunoelectron Microscopy. Isolation of Ribosomal Proteins: B.S. Cooperman, C.J. Weitzmann, and M.A. Buck, Reversed-Phase High-Performance Liquid Chromatography of Ribosomal Proteins. M.S. Capel, D.B. Datta, C.R. Nierras, and G.R. Craven, Ion-Exchange High-Performance Liquid Chromatographic Separation of Ribosomal Proteins. R.M. Kamp and B. Wittmann-Liebold, Ribosomal Proteins from Archaebacteria High-Performance Liquid Chromatographic Purification for Microsequence Analysis. Ribosome Function and Kinetics: J. Krieg, A.R. Olivier, and G. Thomas, Analysis of 40S Ribosomal Protein S6 Phosphorylation during the Mitogenic Response. J.M. Robertson, H. Paulsen, and W. Wintermeyer, Pre-Steady-State Kinetic Studies on Ribosomal Translocation. R. Lill and W. Wintermeyer, Quantitative Indicator Assay of tRNA Binding to the Ribosomal P and A Sites. M. Ehrenberg and C.G. Kurland, Measurement of Translational Kinetic Parameters. A.S. Spirin, N.V. Belitsina, and G.Zh.Y. Tnalina, Ribosomal Synthesis of Polypeptides from Aminoacyl-tRNA without Polynucleotide Template. A. Bartetzko and K.H. Nierhaus, Mg2+/NH4+/Polyamine System for Polyuridine-Dependent Poly(phenylalanine) Synthesis with Near in Vivo Characteristics. H.-J. Rheinberger, U. Geigenmuller, and K.H. Nierhaus, Parameters for the Preparation of Escherichia coli Ribosomes and Ribosomal Subunits Active in tRNA Binding. Genetics: C.D. Sigmund, M. Ettayebi, A. Borden, and E.A. Morgan, Antibiotic Resistance Mutations in Ribosomal RNA Genes of Escherichia coli. D.K. Jemiolo, R. Steen, M.J.R. Stark, and A.E. Dahlberg, Analysis of Plasmid-Coded Ribosomal RNA by Maxicell Techniques. J. Schnier and K. Nishi, Temperature-Sensitive Mutants with Alterations in Ribosomal Protein L24 and Isolation of Intra- and Extragenic Suppressor Mutants. B. Vester, J. Egebjerg, R. Garrett, and J. Christiansen, Primer-Directed Deletions in 5 S Ribosomal RNA. H.U. Gvringer and R. Wagner, 5 S RNA Structure and Function. A. Prombona, Y. Ogihara, and A.R. Subramanian, Cloning and Identification of Ribosomal Protein Genes in Chloroplast DNA. Mathematical and Computer Analysis of Ribosomal Sequences: M.S. Waterman, Computer Analysis of Nucleic Acid Sequences. G.J. Olsen, Phylogenetic Analysis Using Ribosomal RNA. Author Index. Subject Index.
This volume includes a variety of methods involving electron microscopy and other biophysical methods, such as crystallography, neutron scattering, and NMR procedures for the analysis of protein-RNA or RNA-RNA interactions by cross-linking, the use of chemical, enzymatic, and immunological probes, as well as functional and genetic approaches for the study of this nucleoprotein. These methodologies will contribute to the progress toward the elucidation of the structure, function, and regulatory processes that affect this most important complex cellular component, the ribosome.
Biochemists, microbiologists, cell and molecular biologists, biophysicists, geneticists.
- No. of pages:
- © Academic Press 1988
- 28th December 1988
- Academic Press
- eBook ISBN:
@from:Praise for the Volume @qu:"The volume is of a high scientific and technical standard usual for this series and will certainly be of great value as a basic methodological handbook to research specialists involved in biochemical, biophysical and ultrastructural ribosome analysis and related studies." @source:--BIOLOGIA PLANTARUM @from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
University of California, Santa Cruz, U.S.A.
Department of Molecular Biology and Biochemistry, University of California, Irvine, California, U.S.A.
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