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Plant proteomics : technologies, strategies, and applications / / edited by Ganesh Kumar Agrawal, Randeep Rakwal
| Plant proteomics : technologies, strategies, and applications / / edited by Ganesh Kumar Agrawal, Randeep Rakwal |
| Pubbl/distr/stampa | Hoboken, N.J., : J. Wiley, c2008 |
| Descrizione fisica | 1 online resource (818 p.) |
| Disciplina | 572/.62 |
| Altri autori (Persone) |
AgrawalGanesh Kumar
RakwalRandeep |
| Collana | Wiley-Interscience series in mass spectrometry |
| Soggetto topico |
Plant proteins
Plant proteomics |
| ISBN |
1-281-83132-8
9786611831325 0-470-36963-9 0-470-36983-3 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PLANT PROTEOMICS; CONTENTS; PREFACE; CONTRIBUTORS; ACRONYMS AND ABBREVIATIONS; 1 AN INTRODUCTION TO PROTEOMICS: APPLICATIONS TO PLANT BIOLOGY; 1.1 Proteomics Defined; 1.2 Proteomics Applied; References; PART I TECHNOLOGIES; 2 GEL-BASED PROTEOMICS; 2.1 Introduction and Brief Bibliographic Review; 2.2 SDS-PAGE; 2.3 IEF; 2.4 2D Maps; 2.5 Conclusions; 2.6 Five-Year Viewpoint; References; 3 MASS SPECTROMETRY-BASED PROTEOMICS: IDENTIFYING PLANT PROTEINS; 3.1 Introduction and Brief Bibliographic Review; 3.2 Instrumentation; 3.3 MALDI; 3.4 ESI; 3.5 Mass Analyzers; 3.6 Ion Detectors
3.7 Sample Preparation3.8 Protein Identification; 3.9 Conclusions; 3.10 Five-Year Viewpoint; References; 4 CHEMICAL PROTEOMICS; 4.1 Introduction; 4.2 Strategies For Activity-Based Protein Profiling (ABPP); 4.3 Case Study: Development of Molecular Tools Targeting Plant Kinases; 4.4 Conclusions; 4.5 Five-Year Viewpoint; References; 5 THE ARABIDOPSIS LOCALIZOME: SUBCELLULAR PROTEIN LOCALIZATION AND INTERACTIONS IN ARABIDOPSIS; 5.1 Protein Compartmentalization in Plant Cells; 5.2 Experimental Determination of Protein Localization 5.3 In Vivo Imaging Approaches to Protein Localization and Interaction5.4 Plant Cell Cultures for Studying Protein Localization; 5.5 Protein-Protein Interaction In Vivo: FRET; 5.6 Perspectives: Integrating Predictive and Experimental Protein Localization Data; References; 6 SECRETOME: TOWARD DECIPHERING THE SECRETORY PATHWAYS AND BEYOND; 6.1 Introduction and Brief Bibliographic Review; 6.2 Methodology and Strategy; 6.3 A Case Study: In Planta and In Vitro Protein Profiles of Soluble and Secreted Proteins in Rice; 6.4 Conclusions; 6.5 Five-Year Viewpoint; References; 7 PEPTIDOMICS 7.1 Introduction and Brief Bibliographic Review7.2 Separation Technology; 7.3 MS Technology; 7.4 Bioinformatics and Data Mining; 7.5 Differential Peptide Display; 7.6 ID LC-MALDI; 7.7 2D CA-RP-LC-ESI-MS; 7.8 Applications; 7.9 Peptides and Proteases; 7.10 Conclusions; 7.11 Five-Year Viewpoint; References; PART II COMPUTATIONAL PROTEOMICS; 8 BIOINFORMATICS IN GEL-BASED PROTEOMICS; 8.1 Introduction and Brief Bibliographic Review; 8.2 Methodology and Strategy; 8.3 Experimental Results and Applications; 8.4 Conclusions; 8.5 Five-Year Viewpoint; References; 9 BIOINFORMATICS IN MS-BASED PROTEOMICS 9.1 Introduction9.2 Database Searching; 9.3 Peptide De Novo Sequencing; 9.4 Conclusions and Five-Year Viewpoint; References; PART III EXPRESSION PROTEOMICS; 10 AN OVERVIEW OF THE ARABIDOPSIS PROTEOME; 10.1 Introduction and Brief Bibliographic Review; 10.2 Methodology and Strategy; 10.3 Experimental Results and Applications; 10.4 Conclusions; 10.5 Five-Year Viewpoint; References; 11 RICE PROTEOME AT A GLANCE; 11.1 Introduction and Brief Bibliographic Review; 11.2 Methodology and Strategy; 11.3 Experimental Results and Applications; 11.4 Conclusions; 11.5 Five-Year Viewpoint; References 12 PROTEOMICS OF LEGUME PLANTS |
| Record Nr. | UNINA-9910876700303321 |
| Hoboken, N.J., : J. Wiley, c2008 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Plant proteomics [[electronic resource] /] / edited by Christine Finnie
| Plant proteomics [[electronic resource] /] / edited by Christine Finnie |
| Pubbl/distr/stampa | Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 |
| Descrizione fisica | 1 online resource (276 p.) |
| Disciplina |
572.62
572/.62 580.5 |
| Altri autori (Persone) | FinnieChristine |
| Collana | Annual plant reviews |
| Soggetto topico |
Plant proteins
Plant proteomics |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-74882-6
9786610748822 0-470-76427-9 0-470-98887-8 1-4051-7307-6 |
| Classificazione | 42.42 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Plant Proteomics; Contents; Preface; Contributors; 1 Plant proteomics: challenges and resources; 1.1 Introduction; 1.2 Challenges; 1.2.1 Sample extraction; 1.2.1.1 Two-dimensional gel electrophoresis; 1.2.1.2 Direct MS analysis of samples; 1.2.2 Sample preparation and arraying; 1.2.2.1 Two-dimensional gel electrophoresis; 1.2.2.2 One-dimensional gel electrophoresis; 1.2.2.3 Blue-native gel electrophoresis; 1.2.2.4 Direct analysis of samples by MS; 1.2.3 Mass spectrometry (MALDI and ESI); 1.2.3.1 MALDI; 1.2.3.2 ESI; 1.2.4 Analysis depth; 1.2.5 Data analysis; 1.2.5.1 Peptide mass fingerprints
1.2.5.2 Peptide fragmentation data (MS/MS)1.2.5.3 Analysis options; 1.2.6 Quantitation; 1.2.6.1 Gel stains; 1.2.6.2 Chemical labelling of sample; 1.2.7 Modifications; 1.2.8 Data; 1.3 Resources; 1.3.1 Proteomic databases; 1.3.2 Online proteomic tools and resources; 1.4 Future; 2 Proteomic analysis of post-translational modifications by mass spectrometry; 2.1 Summary; 2.2 Introduction; 2.3 Considerations for the experimental design of PTM analysis by proteomics; 2.4 Analysis of PTMs by proteomic approaches; 2.4.1 Phosphorylation; 2.4.2 Protein glycosylation; 2.4.3 GPI-AP; 2.4.4 Farnesylation 2.4.5 N-terminally modified proteins2.5 Conclusions and perspectives; 3 Strategies for the investigation of protein-protein interactions in plants; 3.1 Summary; 3.2 Introduction; 3.3 Biochemical procedures to characterize protein-protein interactions; 3.3.1 Chromatographic purifications; 3.3.2 Sucrose gradient ultrafiltration; 3.3.3 Native gel electrophoresis; 3.3.4 Immunoprecipitations; 3.4 Genetic procedures to characterize protein-protein interactions; 3.4.1 Yeast two-hybrid system; 3.4.2 Yeast three-hybrid system; 3.4.3 Yeast one-hybrid system 3.4.4 Limitations of yeast two-hybrid systems3.4.5 Split-ubiquitin system; 3.4.6 Bimolecular fluorescence complementation (BiFC); 3.4.7 Förster resonance energy transfer (FRET); 3.4.8 Tagging technologies for the purification of protein complexes; 3.5 Cytological procedures to characterize protein-protein interactions; 3.6 Outlook; 4 Proteomics of disulphide and cysteine oxidoreduction; 4.1 Introduction; 4.2 Control of cellular redox status; 4.2.1 Sequence and structural features of proteins catalysing cysteine redox modifications; 4.2.2 Catalytic mechanisms of Trxs and Grxs 4.3 Proteomics techniques for analysis of cysteine modifications4.3.1 Reagents for cysteine labelling; 4.3.2 Disulphide mapping; 4.3.3 S-glutathionylation; 4.3.4 Cysteine SOH, SO2H and SO3H; 4.3.5 Trxs and disulphide reduction; 4.3.6 S-nitrosylation; 4.4 Conclusions and perspectives; 5 Structural proteomics; 5.1 Introduction; 5.2 Project data handling: Sesame; 5.3 ORF cloning; 5.4 E. coli cell-based protein production pipeline; 5.4.1 Large-scale protein production and labeling; 5.4.2 Protein purification; 5.5 Wheat germ cell-free protein production 5.6 Mass spectrometry of purified proteins for quality assurance and analysis |
| Record Nr. | UNINA-9910143294703321 |
| Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Plant proteomics [[electronic resource] /] / edited by Christine Finnie
| Plant proteomics [[electronic resource] /] / edited by Christine Finnie |
| Pubbl/distr/stampa | Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 |
| Descrizione fisica | 1 online resource (276 p.) |
| Disciplina |
572.62
572/.62 580.5 |
| Altri autori (Persone) | FinnieChristine |
| Collana | Annual plant reviews |
| Soggetto topico |
Plant proteins
Plant proteomics |
| ISBN |
1-280-74882-6
9786610748822 0-470-76427-9 0-470-98887-8 1-4051-7307-6 |
| Classificazione | 42.42 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Plant Proteomics; Contents; Preface; Contributors; 1 Plant proteomics: challenges and resources; 1.1 Introduction; 1.2 Challenges; 1.2.1 Sample extraction; 1.2.1.1 Two-dimensional gel electrophoresis; 1.2.1.2 Direct MS analysis of samples; 1.2.2 Sample preparation and arraying; 1.2.2.1 Two-dimensional gel electrophoresis; 1.2.2.2 One-dimensional gel electrophoresis; 1.2.2.3 Blue-native gel electrophoresis; 1.2.2.4 Direct analysis of samples by MS; 1.2.3 Mass spectrometry (MALDI and ESI); 1.2.3.1 MALDI; 1.2.3.2 ESI; 1.2.4 Analysis depth; 1.2.5 Data analysis; 1.2.5.1 Peptide mass fingerprints
1.2.5.2 Peptide fragmentation data (MS/MS)1.2.5.3 Analysis options; 1.2.6 Quantitation; 1.2.6.1 Gel stains; 1.2.6.2 Chemical labelling of sample; 1.2.7 Modifications; 1.2.8 Data; 1.3 Resources; 1.3.1 Proteomic databases; 1.3.2 Online proteomic tools and resources; 1.4 Future; 2 Proteomic analysis of post-translational modifications by mass spectrometry; 2.1 Summary; 2.2 Introduction; 2.3 Considerations for the experimental design of PTM analysis by proteomics; 2.4 Analysis of PTMs by proteomic approaches; 2.4.1 Phosphorylation; 2.4.2 Protein glycosylation; 2.4.3 GPI-AP; 2.4.4 Farnesylation 2.4.5 N-terminally modified proteins2.5 Conclusions and perspectives; 3 Strategies for the investigation of protein-protein interactions in plants; 3.1 Summary; 3.2 Introduction; 3.3 Biochemical procedures to characterize protein-protein interactions; 3.3.1 Chromatographic purifications; 3.3.2 Sucrose gradient ultrafiltration; 3.3.3 Native gel electrophoresis; 3.3.4 Immunoprecipitations; 3.4 Genetic procedures to characterize protein-protein interactions; 3.4.1 Yeast two-hybrid system; 3.4.2 Yeast three-hybrid system; 3.4.3 Yeast one-hybrid system 3.4.4 Limitations of yeast two-hybrid systems3.4.5 Split-ubiquitin system; 3.4.6 Bimolecular fluorescence complementation (BiFC); 3.4.7 Förster resonance energy transfer (FRET); 3.4.8 Tagging technologies for the purification of protein complexes; 3.5 Cytological procedures to characterize protein-protein interactions; 3.6 Outlook; 4 Proteomics of disulphide and cysteine oxidoreduction; 4.1 Introduction; 4.2 Control of cellular redox status; 4.2.1 Sequence and structural features of proteins catalysing cysteine redox modifications; 4.2.2 Catalytic mechanisms of Trxs and Grxs 4.3 Proteomics techniques for analysis of cysteine modifications4.3.1 Reagents for cysteine labelling; 4.3.2 Disulphide mapping; 4.3.3 S-glutathionylation; 4.3.4 Cysteine SOH, SO2H and SO3H; 4.3.5 Trxs and disulphide reduction; 4.3.6 S-nitrosylation; 4.4 Conclusions and perspectives; 5 Structural proteomics; 5.1 Introduction; 5.2 Project data handling: Sesame; 5.3 ORF cloning; 5.4 E. coli cell-based protein production pipeline; 5.4.1 Large-scale protein production and labeling; 5.4.2 Protein purification; 5.5 Wheat germ cell-free protein production 5.6 Mass spectrometry of purified proteins for quality assurance and analysis |
| Record Nr. | UNISA-996213069903316 |
| Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Plant proteomics [[electronic resource] /] / edited by Christine Finnie
| Plant proteomics [[electronic resource] /] / edited by Christine Finnie |
| Pubbl/distr/stampa | Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 |
| Descrizione fisica | 1 online resource (276 p.) |
| Disciplina |
572.62
572/.62 580.5 |
| Altri autori (Persone) | FinnieChristine |
| Collana | Annual plant reviews |
| Soggetto topico |
Plant proteins
Plant proteomics |
| ISBN |
1-280-74882-6
9786610748822 0-470-76427-9 0-470-98887-8 1-4051-7307-6 |
| Classificazione | 42.42 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Plant Proteomics; Contents; Preface; Contributors; 1 Plant proteomics: challenges and resources; 1.1 Introduction; 1.2 Challenges; 1.2.1 Sample extraction; 1.2.1.1 Two-dimensional gel electrophoresis; 1.2.1.2 Direct MS analysis of samples; 1.2.2 Sample preparation and arraying; 1.2.2.1 Two-dimensional gel electrophoresis; 1.2.2.2 One-dimensional gel electrophoresis; 1.2.2.3 Blue-native gel electrophoresis; 1.2.2.4 Direct analysis of samples by MS; 1.2.3 Mass spectrometry (MALDI and ESI); 1.2.3.1 MALDI; 1.2.3.2 ESI; 1.2.4 Analysis depth; 1.2.5 Data analysis; 1.2.5.1 Peptide mass fingerprints
1.2.5.2 Peptide fragmentation data (MS/MS)1.2.5.3 Analysis options; 1.2.6 Quantitation; 1.2.6.1 Gel stains; 1.2.6.2 Chemical labelling of sample; 1.2.7 Modifications; 1.2.8 Data; 1.3 Resources; 1.3.1 Proteomic databases; 1.3.2 Online proteomic tools and resources; 1.4 Future; 2 Proteomic analysis of post-translational modifications by mass spectrometry; 2.1 Summary; 2.2 Introduction; 2.3 Considerations for the experimental design of PTM analysis by proteomics; 2.4 Analysis of PTMs by proteomic approaches; 2.4.1 Phosphorylation; 2.4.2 Protein glycosylation; 2.4.3 GPI-AP; 2.4.4 Farnesylation 2.4.5 N-terminally modified proteins2.5 Conclusions and perspectives; 3 Strategies for the investigation of protein-protein interactions in plants; 3.1 Summary; 3.2 Introduction; 3.3 Biochemical procedures to characterize protein-protein interactions; 3.3.1 Chromatographic purifications; 3.3.2 Sucrose gradient ultrafiltration; 3.3.3 Native gel electrophoresis; 3.3.4 Immunoprecipitations; 3.4 Genetic procedures to characterize protein-protein interactions; 3.4.1 Yeast two-hybrid system; 3.4.2 Yeast three-hybrid system; 3.4.3 Yeast one-hybrid system 3.4.4 Limitations of yeast two-hybrid systems3.4.5 Split-ubiquitin system; 3.4.6 Bimolecular fluorescence complementation (BiFC); 3.4.7 Förster resonance energy transfer (FRET); 3.4.8 Tagging technologies for the purification of protein complexes; 3.5 Cytological procedures to characterize protein-protein interactions; 3.6 Outlook; 4 Proteomics of disulphide and cysteine oxidoreduction; 4.1 Introduction; 4.2 Control of cellular redox status; 4.2.1 Sequence and structural features of proteins catalysing cysteine redox modifications; 4.2.2 Catalytic mechanisms of Trxs and Grxs 4.3 Proteomics techniques for analysis of cysteine modifications4.3.1 Reagents for cysteine labelling; 4.3.2 Disulphide mapping; 4.3.3 S-glutathionylation; 4.3.4 Cysteine SOH, SO2H and SO3H; 4.3.5 Trxs and disulphide reduction; 4.3.6 S-nitrosylation; 4.4 Conclusions and perspectives; 5 Structural proteomics; 5.1 Introduction; 5.2 Project data handling: Sesame; 5.3 ORF cloning; 5.4 E. coli cell-based protein production pipeline; 5.4.1 Large-scale protein production and labeling; 5.4.2 Protein purification; 5.5 Wheat germ cell-free protein production 5.6 Mass spectrometry of purified proteins for quality assurance and analysis |
| Record Nr. | UNINA-9910829864203321 |
| Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Plant proteomics / / edited by Christine Finnie
| Plant proteomics / / edited by Christine Finnie |
| Pubbl/distr/stampa | Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 |
| Descrizione fisica | 1 online resource (276 p.) |
| Disciplina | 572/.62 |
| Altri autori (Persone) | FinnieChristine |
| Collana | Annual plant reviews |
| Soggetto topico |
Plant proteins
Plant proteomics |
| ISBN |
1-280-74882-6
9786610748822 0-470-76427-9 0-470-98887-8 1-4051-7307-6 |
| Classificazione | 42.42 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Plant Proteomics; Contents; Preface; Contributors; 1 Plant proteomics: challenges and resources; 1.1 Introduction; 1.2 Challenges; 1.2.1 Sample extraction; 1.2.1.1 Two-dimensional gel electrophoresis; 1.2.1.2 Direct MS analysis of samples; 1.2.2 Sample preparation and arraying; 1.2.2.1 Two-dimensional gel electrophoresis; 1.2.2.2 One-dimensional gel electrophoresis; 1.2.2.3 Blue-native gel electrophoresis; 1.2.2.4 Direct analysis of samples by MS; 1.2.3 Mass spectrometry (MALDI and ESI); 1.2.3.1 MALDI; 1.2.3.2 ESI; 1.2.4 Analysis depth; 1.2.5 Data analysis; 1.2.5.1 Peptide mass fingerprints
1.2.5.2 Peptide fragmentation data (MS/MS)1.2.5.3 Analysis options; 1.2.6 Quantitation; 1.2.6.1 Gel stains; 1.2.6.2 Chemical labelling of sample; 1.2.7 Modifications; 1.2.8 Data; 1.3 Resources; 1.3.1 Proteomic databases; 1.3.2 Online proteomic tools and resources; 1.4 Future; 2 Proteomic analysis of post-translational modifications by mass spectrometry; 2.1 Summary; 2.2 Introduction; 2.3 Considerations for the experimental design of PTM analysis by proteomics; 2.4 Analysis of PTMs by proteomic approaches; 2.4.1 Phosphorylation; 2.4.2 Protein glycosylation; 2.4.3 GPI-AP; 2.4.4 Farnesylation 2.4.5 N-terminally modified proteins2.5 Conclusions and perspectives; 3 Strategies for the investigation of protein-protein interactions in plants; 3.1 Summary; 3.2 Introduction; 3.3 Biochemical procedures to characterize protein-protein interactions; 3.3.1 Chromatographic purifications; 3.3.2 Sucrose gradient ultrafiltration; 3.3.3 Native gel electrophoresis; 3.3.4 Immunoprecipitations; 3.4 Genetic procedures to characterize protein-protein interactions; 3.4.1 Yeast two-hybrid system; 3.4.2 Yeast three-hybrid system; 3.4.3 Yeast one-hybrid system 3.4.4 Limitations of yeast two-hybrid systems3.4.5 Split-ubiquitin system; 3.4.6 Bimolecular fluorescence complementation (BiFC); 3.4.7 Förster resonance energy transfer (FRET); 3.4.8 Tagging technologies for the purification of protein complexes; 3.5 Cytological procedures to characterize protein-protein interactions; 3.6 Outlook; 4 Proteomics of disulphide and cysteine oxidoreduction; 4.1 Introduction; 4.2 Control of cellular redox status; 4.2.1 Sequence and structural features of proteins catalysing cysteine redox modifications; 4.2.2 Catalytic mechanisms of Trxs and Grxs 4.3 Proteomics techniques for analysis of cysteine modifications4.3.1 Reagents for cysteine labelling; 4.3.2 Disulphide mapping; 4.3.3 S-glutathionylation; 4.3.4 Cysteine SOH, SO2H and SO3H; 4.3.5 Trxs and disulphide reduction; 4.3.6 S-nitrosylation; 4.4 Conclusions and perspectives; 5 Structural proteomics; 5.1 Introduction; 5.2 Project data handling: Sesame; 5.3 ORF cloning; 5.4 E. coli cell-based protein production pipeline; 5.4.1 Large-scale protein production and labeling; 5.4.2 Protein purification; 5.5 Wheat germ cell-free protein production 5.6 Mass spectrometry of purified proteins for quality assurance and analysis |
| Record Nr. | UNINA-9910876685503321 |
| Oxford, UK ; ; Ames, Iowa, : Blackwell Pub., 2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteomics of biological systems [[electronic resource] ] : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham
| Proteomics of biological systems [[electronic resource] ] : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
| Autore | Ham Bryan M |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
| Descrizione fisica | 1 online resource (376 p.) |
| Disciplina | 572/.62 |
| Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
| ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
| Record Nr. | UNINA-9910139593603321 |
Ham Bryan M
|
||
| Hoboken, N.J., : John Wiley & Sons, 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteomics of biological systems : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham
| Proteomics of biological systems : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
| Autore | Ham Bryan M |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
| Descrizione fisica | 1 online resource (376 p.) |
| Disciplina | 572/.62 |
| Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
| ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
| Record Nr. | UNINA-9910821480603321 |
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Ham Bryan M
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| Hoboken, N.J., : John Wiley & Sons, 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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