The Ninth International Conference on Methods in Protein Sequence Analysis was held for the first time in Asia from September 20 to September 24, 1992 in Otsu (a city near Kyoto), Japan. Approximately 400 delegates attended the meeting. Forty papers were presented orally and 147 poster presentations were discussed. Academic sessions were held from early in the morning until late in the evening. We are confident that the Conference was successful in providing up-to-date information about methods in protein sequence analysis to all participants. Moreover, with the knowledge and understanding of…mehr
The Ninth International Conference on Methods in Protein Sequence Analysis was held for the first time in Asia from September 20 to September 24, 1992 in Otsu (a city near Kyoto), Japan. Approximately 400 delegates attended the meeting. Forty papers were presented orally and 147 poster presentations were discussed. Academic sessions were held from early in the morning until late in the evening. We are confident that the Conference was successful in providing up-to-date information about methods in protein sequence analysis to all participants. Moreover, with the knowledge and understanding of the present standard of various methods of analysis that are being used and will be used, we were able to clarify areas that need to be evaluated, to be improved and be explored further. Major topics in the Conference mostly covered areas in the methodology of protein sequence analysis, such as: micropreparation and microsequencing of proteins, mass spectrometry, post-translational modification, prediction and database analysis, and analysis of protein structures of special interests. The evolution of genetic engineering in molecular biology has greatly accelerated the accumulation of knowledge on the amino acid sequence of novel proteins regardless of whether they are expressed or not expressed in living organisms. In the early stage of accumulation of structural information, the amino acid sequence itself is worthy of notice.
Micropreparation and Microsequencing.- Capillary liquid chromatography: a tool for protein structural analysis.- Routine amino acid sequencing on 2D-gel separated proteins: a protein elution and concentration gel system.- Capillary electrophoresis in structural characterization of polypeptides.- Sensitization of gas-phase protein sequencer using fluorescein isothiocyanate (FITC).- Thiobenzoylation method of protein sequencing: gas chromatography/ mass spectrometric detection of 5-acetoxy-2-phenylthiazoles.- Deblocking and subsequent microsequence analysis of N-terminally blocked proteins immobilized on PVDF membrane.- Development of novel C-terminal sequencing methods.- Automated C-terminal sequencing of peptides and proteins.- A new chemical approach to C-terminal microsequence analysis via the thiohydantoin.- Cyanogen bromide cleavage of proteins on blots and subsequent separation of the fragments by polyacrylamide gel electrophoresis directly from those blots.- Identification of the disulfide bonds of the human complement component C3.- A novel protease from jack-bean seeds: asparaginyl endopeptidase.- Lysine-specific serine protease from Achromobacter lyticus: its substrate specificity and comparison with trypsin.- Structure and function of snake venom metalloproteinase family.- Mass Spectrometry.- Recent advances in protein sequencing by mass spectrometry. Introduction and overview.- Sequence analysis of peptides presented to the immune system by class I and class IIMHC molecules.- High precision mass spectrometry with the ion trap mass spectrometer.- Electrospray-mass spectrometry, an emerging methodology for elucidating structure-function relationships of proteins.- A general strategy for the use of mass spectrometric molecular weight information in protein purification and sequence determination.- Determination of posttranslational modifications by mass spectrometry.- Post-Translational Modifications.- Post-translational modifications of proteins.- N-Terminal acetylation of mutationally altered form of iso-1-cytochromes c in normal and natl- strains deficient in the major N-terminal acetyl transferase of the yeast Saccharomyces cerevisiae.- Posttranslational glutamylation of several brain tubulin isotypes: structure of the polyglutamyl side chain.- Protein anchoring to membrane by glycosylphosphatidylinositol: Determination of the COOH-terminal signal peptide sequence and GPI-attachment site in bovine liver 5?-nucleotidase.- Pyridylamination for sensitive analysis of sugar chains of glycoproteins.- Sequence analysis of phosphopeptides and its application for the determination of phosphorylated sites of proteins.- Prediction and Database Analysis.- Prediction of protein structure from multiple sequence alignment.- Sequence patterns that characterize protein families with a common fold.- Domains and modules of proteins.- Homology search and prediction of biological function of protein from amino acid sequences.- Amino acid sequence comparison as an aid to determining evolutionary origins.- Protein databases constructed by quantitative two-dimensional gel electrophoresis.- Protein Structures of Special Interests.- Biochemistry of a natriuretic peptide family.- Activin, activin-binding protein (follistatin) and activin receptor.- Do well-populated intermediates represent the pathway of protein folding?.- Alcohol dehydrogenases: patterns of protein evolution.- Structure and post-translational modification of the lipoyl domain of 2-oxo acid dehydrogenase complexes: a new family of protein domains.- Structure analysis of thetopography and molecular organization of protein-RNA complexes as revealed in ribosomes.
Micropreparation and Microsequencing.- Capillary liquid chromatography: a tool for protein structural analysis.- Routine amino acid sequencing on 2D-gel separated proteins: a protein elution and concentration gel system.- Capillary electrophoresis in structural characterization of polypeptides.- Sensitization of gas-phase protein sequencer using fluorescein isothiocyanate (FITC).- Thiobenzoylation method of protein sequencing: gas chromatography/ mass spectrometric detection of 5-acetoxy-2-phenylthiazoles.- Deblocking and subsequent microsequence analysis of N-terminally blocked proteins immobilized on PVDF membrane.- Development of novel C-terminal sequencing methods.- Automated C-terminal sequencing of peptides and proteins.- A new chemical approach to C-terminal microsequence analysis via the thiohydantoin.- Cyanogen bromide cleavage of proteins on blots and subsequent separation of the fragments by polyacrylamide gel electrophoresis directly from those blots.- Identification of the disulfide bonds of the human complement component C3.- A novel protease from jack-bean seeds: asparaginyl endopeptidase.- Lysine-specific serine protease from Achromobacter lyticus: its substrate specificity and comparison with trypsin.- Structure and function of snake venom metalloproteinase family.- Mass Spectrometry.- Recent advances in protein sequencing by mass spectrometry. Introduction and overview.- Sequence analysis of peptides presented to the immune system by class I and class IIMHC molecules.- High precision mass spectrometry with the ion trap mass spectrometer.- Electrospray-mass spectrometry, an emerging methodology for elucidating structure-function relationships of proteins.- A general strategy for the use of mass spectrometric molecular weight information in protein purification and sequence determination.- Determination of posttranslational modifications by mass spectrometry.- Post-Translational Modifications.- Post-translational modifications of proteins.- N-Terminal acetylation of mutationally altered form of iso-1-cytochromes c in normal and natl- strains deficient in the major N-terminal acetyl transferase of the yeast Saccharomyces cerevisiae.- Posttranslational glutamylation of several brain tubulin isotypes: structure of the polyglutamyl side chain.- Protein anchoring to membrane by glycosylphosphatidylinositol: Determination of the COOH-terminal signal peptide sequence and GPI-attachment site in bovine liver 5?-nucleotidase.- Pyridylamination for sensitive analysis of sugar chains of glycoproteins.- Sequence analysis of phosphopeptides and its application for the determination of phosphorylated sites of proteins.- Prediction and Database Analysis.- Prediction of protein structure from multiple sequence alignment.- Sequence patterns that characterize protein families with a common fold.- Domains and modules of proteins.- Homology search and prediction of biological function of protein from amino acid sequences.- Amino acid sequence comparison as an aid to determining evolutionary origins.- Protein databases constructed by quantitative two-dimensional gel electrophoresis.- Protein Structures of Special Interests.- Biochemistry of a natriuretic peptide family.- Activin, activin-binding protein (follistatin) and activin receptor.- Do well-populated intermediates represent the pathway of protein folding?.- Alcohol dehydrogenases: patterns of protein evolution.- Structure and post-translational modification of the lipoyl domain of 2-oxo acid dehydrogenase complexes: a new family of protein domains.- Structure analysis of thetopography and molecular organization of protein-RNA complexes as revealed in ribosomes.
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