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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 | ||
| ||