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Application of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics : A Replacement for Western Blot Analysis / / by Michael Kinter, Caroline S. Kinter
| Application of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics : A Replacement for Western Blot Analysis / / by Michael Kinter, Caroline S. Kinter |
| Autore | Kinter Michael |
| Edizione | [1st ed. 2013.] |
| Pubbl/distr/stampa | New York, NY : , : Springer New York : , : Imprint : Springer, , 2013 |
| Descrizione fisica | 1 online resource (76 p.) |
| Disciplina | 610 |
| Collana | SpringerBriefs in Systems Biology |
| Soggetto topico |
Medicine
Proteomics Mass spectrometry Biochemistry Biomedicine, general Mass Spectrometry Biochemistry, general |
| ISBN | 1-4614-8666-1 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | The use of mass spectrometry for highly selective detection -- overview of how the selected reaction monitoring experiment works -- Designing a selected reaction monitoring method for a protein -- Example analyses include: sample processing, sample analysis, data processing -- Future Directions. |
| Record Nr. | UNINA-9910437827903321 |
Kinter Michael
|
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| New York, NY : , : Springer New York : , : Imprint : Springer, , 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein sequencing and identification using tandem mass spectrometry [[electronic resource] /] / Michael Kinter, Nicholas E. Sherman
| Protein sequencing and identification using tandem mass spectrometry [[electronic resource] /] / Michael Kinter, Nicholas E. Sherman |
| Autore | Kinter Michael |
| Pubbl/distr/stampa | New York, : Wiley-Interscience, c2000 |
| Descrizione fisica | 1 online resource (321 p.) |
| Disciplina | 572.85 |
| Altri autori (Persone) | ShermanNicholas E |
| Collana | Wiley-Interscience series on mass spectrometry |
| Soggetto topico |
Nucleotide sequence
Proteins Mass spectrometry |
| ISBN |
1-280-54166-0
9786610541669 0-471-23188-6 0-471-72198-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEIN SEQUENCING AND IDENTIFICATION USING TANDEM MASS SPECTROMETRY; CONTENTS; Series Preface; Preface; Chapter 1. An Introduction to Protein Sequencing Using Tandem Mass Spectrometry; 1.1. Introduction; 1.2. References; Chapter 2. The Primary Structure of Proteins and a Historical Overview of Protein Sequencing; 2.1. Protein and Peptide Structure; 2.2. Edman Degradation; 2.2.1. The Edman Reaction; 2.2.2. Incorporation of the Edman Degradation Reaction into Automated Protein Sequenators; 2.2.3. Edman Degradation in Proteomic Research; 2.3. Tandem Mass Spectrometry
2.3.1. A Brief History of the Application of Mass Spectrometry to Protein Sequencing2.3.2. Sequence Analysis of Peptides Using Electron Ionization Mass Spectrometry; 2.3.3. The Utilization of Fast Atom Bombardment with Tandem Mass Spectrometry to Sequence Peptides; 2.3.4. Internal Sequence Analysis of Proteins Using Electrospray Ionization-Tandem Mass Spectrometry and Matrix-Assisted Laser Desorption/Ionization-Time-of- Flight Mass Spectrometry; 2.4. Summary; 2.5. References; Chapter 3. Fundamental Mass Spectrometry; 3.1. An Overview of the Instrumentation; 3.2. Ionization Methods 3.2.1. Electrospray Ionization3.2.2. Nanospray and Microspray Ionization; 3.2.3. Matrix-Assisted Laser Desorption/ Ionization; 3.3. Mass Analyzers; 3.3.1. Fundamental Parameters of Mass Analysis; 3.3.2. Quadrupole Mass Filters (3.20); 3.3.3. Ion Trap Mass Analyzers (3.21-3.23); 3.3.4. Time-of-Flight Mass Analyzers (3.5); 3.4. Tandem Mass Spectrometry; 3.4.1. Collisionally Induced Dissociation; 3.4.2. Tandem Mass Spectrometers; 3.4.3. Types of Tandem Mass Spectrometry Experiments; 3.5. Data Systems; 3.6. Summary; 3.7. References Chapter 4. Collisionally Induced Dissociation of Protonated Peptide Ions and the Interpretation of Product Ion Spectra4.1. Introduction; 4.2. Peptide Fragmentation Chemistry; 4.2.1. Collisionally Induced Dissociation of Peptide Ions Formed by Electrospray Ionization; 4.2.2. Fragmentation of Protonated Peptide Ions Formed by Matrix-Assisted Laser Desorption/Ionization; 4.3. Interpretation of the Product Ion Spectra of Tryptic Peptides; 4.3.1. Tabulated Values Used in the Interpretation; 4.3.2. A Strategy for the Interpretation of Product Ion Spectra of Tryptic Peptides 4.3.3. Sample Interpretation Problem Number One4.3.4. Sample Interpretation Problem Number Two; 4.3.5. A Summary of Interpretation Problems One and Two; 4.3.6. Examples of More Difficult Product Ion Spectra That Cannot Be Completely Interpreted; 4.3.7. Interpretation of Product Ion Spectra from Triply Charged Ions; 4.4. Summary; 4.5. References; Chapter 5. Basic Polyacrylamide Gel Electrophoresis; 5.1. Introduction; 5.2. The Principles of Gel Electrophoresis; 5.2.1. Protein Movement and Separation; 5.2.2. Protein Detection 5.3. The Basic Steps in a Polyacrylamide Gel Electrophoresis Experiment |
| Record Nr. | UNINA-9910146071003321 |
|
Kinter Michael
|
||
| New York, : Wiley-Interscience, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein sequencing and identification using tandem mass spectrometry [[electronic resource] /] / Michael Kinter, Nicholas E. Sherman
| Protein sequencing and identification using tandem mass spectrometry [[electronic resource] /] / Michael Kinter, Nicholas E. Sherman |
| Autore | Kinter Michael |
| Pubbl/distr/stampa | New York, : Wiley-Interscience, c2000 |
| Descrizione fisica | 1 online resource (321 p.) |
| Disciplina | 572.85 |
| Altri autori (Persone) | ShermanNicholas E |
| Collana | Wiley-Interscience series on mass spectrometry |
| Soggetto topico |
Nucleotide sequence
Proteins Mass spectrometry |
| ISBN |
1-280-54166-0
9786610541669 0-471-23188-6 0-471-72198-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEIN SEQUENCING AND IDENTIFICATION USING TANDEM MASS SPECTROMETRY; CONTENTS; Series Preface; Preface; Chapter 1. An Introduction to Protein Sequencing Using Tandem Mass Spectrometry; 1.1. Introduction; 1.2. References; Chapter 2. The Primary Structure of Proteins and a Historical Overview of Protein Sequencing; 2.1. Protein and Peptide Structure; 2.2. Edman Degradation; 2.2.1. The Edman Reaction; 2.2.2. Incorporation of the Edman Degradation Reaction into Automated Protein Sequenators; 2.2.3. Edman Degradation in Proteomic Research; 2.3. Tandem Mass Spectrometry
2.3.1. A Brief History of the Application of Mass Spectrometry to Protein Sequencing2.3.2. Sequence Analysis of Peptides Using Electron Ionization Mass Spectrometry; 2.3.3. The Utilization of Fast Atom Bombardment with Tandem Mass Spectrometry to Sequence Peptides; 2.3.4. Internal Sequence Analysis of Proteins Using Electrospray Ionization-Tandem Mass Spectrometry and Matrix-Assisted Laser Desorption/Ionization-Time-of- Flight Mass Spectrometry; 2.4. Summary; 2.5. References; Chapter 3. Fundamental Mass Spectrometry; 3.1. An Overview of the Instrumentation; 3.2. Ionization Methods 3.2.1. Electrospray Ionization3.2.2. Nanospray and Microspray Ionization; 3.2.3. Matrix-Assisted Laser Desorption/ Ionization; 3.3. Mass Analyzers; 3.3.1. Fundamental Parameters of Mass Analysis; 3.3.2. Quadrupole Mass Filters (3.20); 3.3.3. Ion Trap Mass Analyzers (3.21-3.23); 3.3.4. Time-of-Flight Mass Analyzers (3.5); 3.4. Tandem Mass Spectrometry; 3.4.1. Collisionally Induced Dissociation; 3.4.2. Tandem Mass Spectrometers; 3.4.3. Types of Tandem Mass Spectrometry Experiments; 3.5. Data Systems; 3.6. Summary; 3.7. References Chapter 4. Collisionally Induced Dissociation of Protonated Peptide Ions and the Interpretation of Product Ion Spectra4.1. Introduction; 4.2. Peptide Fragmentation Chemistry; 4.2.1. Collisionally Induced Dissociation of Peptide Ions Formed by Electrospray Ionization; 4.2.2. Fragmentation of Protonated Peptide Ions Formed by Matrix-Assisted Laser Desorption/Ionization; 4.3. Interpretation of the Product Ion Spectra of Tryptic Peptides; 4.3.1. Tabulated Values Used in the Interpretation; 4.3.2. A Strategy for the Interpretation of Product Ion Spectra of Tryptic Peptides 4.3.3. Sample Interpretation Problem Number One4.3.4. Sample Interpretation Problem Number Two; 4.3.5. A Summary of Interpretation Problems One and Two; 4.3.6. Examples of More Difficult Product Ion Spectra That Cannot Be Completely Interpreted; 4.3.7. Interpretation of Product Ion Spectra from Triply Charged Ions; 4.4. Summary; 4.5. References; Chapter 5. Basic Polyacrylamide Gel Electrophoresis; 5.1. Introduction; 5.2. The Principles of Gel Electrophoresis; 5.2.1. Protein Movement and Separation; 5.2.2. Protein Detection 5.3. The Basic Steps in a Polyacrylamide Gel Electrophoresis Experiment |
| Record Nr. | UNINA-9910830782503321 |
|
Kinter Michael
|
||
| New York, : Wiley-Interscience, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein sequencing and identification using tandem mass spectrometry / / Michael Kinter, Nicholas E. Sherman
| Protein sequencing and identification using tandem mass spectrometry / / Michael Kinter, Nicholas E. Sherman |
| Autore | Kinter Michael |
| Pubbl/distr/stampa | New York, : Wiley-Interscience, c2000 |
| Descrizione fisica | 1 online resource (321 p.) |
| Disciplina | 572.8/5 |
| Altri autori (Persone) | ShermanNicholas E |
| Collana | Wiley-Interscience series on mass spectrometry |
| Soggetto topico |
Nucleotide sequence
Proteins Mass spectrometry |
| ISBN |
1-280-54166-0
9786610541669 0-471-23188-6 0-471-72198-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEIN SEQUENCING AND IDENTIFICATION USING TANDEM MASS SPECTROMETRY; CONTENTS; Series Preface; Preface; Chapter 1. An Introduction to Protein Sequencing Using Tandem Mass Spectrometry; 1.1. Introduction; 1.2. References; Chapter 2. The Primary Structure of Proteins and a Historical Overview of Protein Sequencing; 2.1. Protein and Peptide Structure; 2.2. Edman Degradation; 2.2.1. The Edman Reaction; 2.2.2. Incorporation of the Edman Degradation Reaction into Automated Protein Sequenators; 2.2.3. Edman Degradation in Proteomic Research; 2.3. Tandem Mass Spectrometry
2.3.1. A Brief History of the Application of Mass Spectrometry to Protein Sequencing2.3.2. Sequence Analysis of Peptides Using Electron Ionization Mass Spectrometry; 2.3.3. The Utilization of Fast Atom Bombardment with Tandem Mass Spectrometry to Sequence Peptides; 2.3.4. Internal Sequence Analysis of Proteins Using Electrospray Ionization-Tandem Mass Spectrometry and Matrix-Assisted Laser Desorption/Ionization-Time-of- Flight Mass Spectrometry; 2.4. Summary; 2.5. References; Chapter 3. Fundamental Mass Spectrometry; 3.1. An Overview of the Instrumentation; 3.2. Ionization Methods 3.2.1. Electrospray Ionization3.2.2. Nanospray and Microspray Ionization; 3.2.3. Matrix-Assisted Laser Desorption/ Ionization; 3.3. Mass Analyzers; 3.3.1. Fundamental Parameters of Mass Analysis; 3.3.2. Quadrupole Mass Filters (3.20); 3.3.3. Ion Trap Mass Analyzers (3.21-3.23); 3.3.4. Time-of-Flight Mass Analyzers (3.5); 3.4. Tandem Mass Spectrometry; 3.4.1. Collisionally Induced Dissociation; 3.4.2. Tandem Mass Spectrometers; 3.4.3. Types of Tandem Mass Spectrometry Experiments; 3.5. Data Systems; 3.6. Summary; 3.7. References Chapter 4. Collisionally Induced Dissociation of Protonated Peptide Ions and the Interpretation of Product Ion Spectra4.1. Introduction; 4.2. Peptide Fragmentation Chemistry; 4.2.1. Collisionally Induced Dissociation of Peptide Ions Formed by Electrospray Ionization; 4.2.2. Fragmentation of Protonated Peptide Ions Formed by Matrix-Assisted Laser Desorption/Ionization; 4.3. Interpretation of the Product Ion Spectra of Tryptic Peptides; 4.3.1. Tabulated Values Used in the Interpretation; 4.3.2. A Strategy for the Interpretation of Product Ion Spectra of Tryptic Peptides 4.3.3. Sample Interpretation Problem Number One4.3.4. Sample Interpretation Problem Number Two; 4.3.5. A Summary of Interpretation Problems One and Two; 4.3.6. Examples of More Difficult Product Ion Spectra That Cannot Be Completely Interpreted; 4.3.7. Interpretation of Product Ion Spectra from Triply Charged Ions; 4.4. Summary; 4.5. References; Chapter 5. Basic Polyacrylamide Gel Electrophoresis; 5.1. Introduction; 5.2. The Principles of Gel Electrophoresis; 5.2.1. Protein Movement and Separation; 5.2.2. Protein Detection 5.3. The Basic Steps in a Polyacrylamide Gel Electrophoresis Experiment |
| Record Nr. | UNINA-9910877595903321 |
|
Kinter Michael
|
||
| New York, : Wiley-Interscience, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||