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Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.]
| Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.] |
| Autore | Eidhammer Ingvar |
| Pubbl/distr/stampa | Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 |
| Descrizione fisica | 1 online resource (356 p.) |
| Disciplina |
572.636
572/.636 |
| Altri autori (Persone) |
BarsnesHarald
EideGeir Egil MartensLennart |
| Soggetto topico |
Proteomics - Statistical methods
Mass spectrometry - Data processing |
| ISBN |
1-118-49404-0
1-299-18826-5 1-118-49378-8 1-118-49377-X |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational and Statistical Methods for Protein Quantification by Mass Spectrometry; Contents; Preface; Terminology; Acknowledgements; 1 Introduction; 1.1 The composition of an organism; 1.1.1 A simple model of an organism; 1.1.2 Composition of cells; 1.2 Homeostasis, physiology, and pathology; 1.3 Protein synthesis; 1.4 Site, sample, state, and environment; 1.5 Abundance and expression - protein and proteome profiles; 1.5.1 The protein dynamic range; 1.6 The importance of exact specification of sites and states; 1.6.1 Biological features; 1.6.2 Physiological and pathological features
1.6.3 Input features1.6.4 External features; 1.6.5 Activity features; 1.6.6 The cell cycle; 1.7 Relative and absolute quantification; 1.7.1 Relative quantification; 1.7.2 Absolute quantification; 1.8 In vivo and in vitro experiments; 1.9 Goals for quantitative protein experiments; 1.10 Exercises; 2 Correlations of mRNA and protein abundances; 2.1 Investigating the correlation; 2.2 Codon bias; 2.3 Main results from experiments; 2.4 The ideal case for mRNA-protein comparison; 2.5 Exploring correlation across genes; 2.6 Exploring correlation within one gene; 2.7 Correlation across subsets 2.8 Comparing mRNA and protein abundances across genes from two situations2.9 Exercises; 2.10 Bibliographic notes; 3 Protein level quantification; 3.1 Two-dimensional gels; 3.1.1 Comparing results from different experiments - DIGE; 3.2 Protein arrays; 3.2.1 Forward arrays; 3.2.2 Reverse arrays; 3.2.3 Detection of binding molecules; 3.2.4 Analysis of protein array readouts; 3.3 Western blotting; 3.4 ELISA - Enzyme-Linked Immunosorbent Assay; 3.5 Bibliographic notes; 4 Mass spectrometry and protein identification; 4.1 Mass spectrometry; 4.1.1 Peptide mass fingerprinting (PMF) 4.1.2 MS/MS - tandem MS4.1.3 Mass spectrometers; 4.2 Isotope composition of peptides; 4.2.1 Predicting the isotope intensity distribution; 4.2.2 Estimating the charge; 4.2.3 Revealing isotope patterns; 4.3 Presenting the intensities - the spectra; 4.4 Peak intensity calculation; 4.5 Peptide identification by MS/MS spectra; 4.5.1 Spectral comparison; 4.5.2 Sequential comparison; 4.5.3 Scoring; 4.5.4 Statistical significance; 4.6 The protein inference problem; 4.6.1 Determining maximal explanatory sets; 4.6.2 Determining minimal explanatory sets; 4.7 False discovery rate for the identifications 4.7.1 Constructing the decoy database4.7.2 Separate or composite search; 4.8 Exercises; 4.9 Bibliographic notes; 5 Protein quantification by mass spectrometry; 5.1 Situations, protein, and peptide variants; 5.1.1 Situation; 5.1.2 Protein variants - peptide variants; 5.2 Replicates; 5.3 Run - experiment - project; 5.3.1 LC-MS/MS run; 5.3.2 Quantification run; 5.3.3 Quantification experiment; 5.3.4 Quantification project; 5.3.5 Planning quantification experiments; 5.4 Comparing quantification approaches/methods; 5.4.1 Accuracy; 5.4.2 Precision; 5.4.3 Repeatability and reproducibility 5.4.4 Dynamic range and linear dynamic range |
| Record Nr. | UNINA-9910141482703321 |
Eidhammer Ingvar
|
||
| Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.]
| Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.] |
| Autore | Eidhammer Ingvar |
| Pubbl/distr/stampa | Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 |
| Descrizione fisica | 1 online resource (356 p.) |
| Disciplina |
572.636
572/.636 |
| Altri autori (Persone) |
BarsnesHarald
EideGeir Egil MartensLennart |
| Soggetto topico |
Proteomics - Statistical methods
Mass spectrometry - Data processing |
| ISBN |
1-118-49404-0
1-299-18826-5 1-118-49378-8 1-118-49377-X |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational and Statistical Methods for Protein Quantification by Mass Spectrometry; Contents; Preface; Terminology; Acknowledgements; 1 Introduction; 1.1 The composition of an organism; 1.1.1 A simple model of an organism; 1.1.2 Composition of cells; 1.2 Homeostasis, physiology, and pathology; 1.3 Protein synthesis; 1.4 Site, sample, state, and environment; 1.5 Abundance and expression - protein and proteome profiles; 1.5.1 The protein dynamic range; 1.6 The importance of exact specification of sites and states; 1.6.1 Biological features; 1.6.2 Physiological and pathological features
1.6.3 Input features1.6.4 External features; 1.6.5 Activity features; 1.6.6 The cell cycle; 1.7 Relative and absolute quantification; 1.7.1 Relative quantification; 1.7.2 Absolute quantification; 1.8 In vivo and in vitro experiments; 1.9 Goals for quantitative protein experiments; 1.10 Exercises; 2 Correlations of mRNA and protein abundances; 2.1 Investigating the correlation; 2.2 Codon bias; 2.3 Main results from experiments; 2.4 The ideal case for mRNA-protein comparison; 2.5 Exploring correlation across genes; 2.6 Exploring correlation within one gene; 2.7 Correlation across subsets 2.8 Comparing mRNA and protein abundances across genes from two situations2.9 Exercises; 2.10 Bibliographic notes; 3 Protein level quantification; 3.1 Two-dimensional gels; 3.1.1 Comparing results from different experiments - DIGE; 3.2 Protein arrays; 3.2.1 Forward arrays; 3.2.2 Reverse arrays; 3.2.3 Detection of binding molecules; 3.2.4 Analysis of protein array readouts; 3.3 Western blotting; 3.4 ELISA - Enzyme-Linked Immunosorbent Assay; 3.5 Bibliographic notes; 4 Mass spectrometry and protein identification; 4.1 Mass spectrometry; 4.1.1 Peptide mass fingerprinting (PMF) 4.1.2 MS/MS - tandem MS4.1.3 Mass spectrometers; 4.2 Isotope composition of peptides; 4.2.1 Predicting the isotope intensity distribution; 4.2.2 Estimating the charge; 4.2.3 Revealing isotope patterns; 4.3 Presenting the intensities - the spectra; 4.4 Peak intensity calculation; 4.5 Peptide identification by MS/MS spectra; 4.5.1 Spectral comparison; 4.5.2 Sequential comparison; 4.5.3 Scoring; 4.5.4 Statistical significance; 4.6 The protein inference problem; 4.6.1 Determining maximal explanatory sets; 4.6.2 Determining minimal explanatory sets; 4.7 False discovery rate for the identifications 4.7.1 Constructing the decoy database4.7.2 Separate or composite search; 4.8 Exercises; 4.9 Bibliographic notes; 5 Protein quantification by mass spectrometry; 5.1 Situations, protein, and peptide variants; 5.1.1 Situation; 5.1.2 Protein variants - peptide variants; 5.2 Replicates; 5.3 Run - experiment - project; 5.3.1 LC-MS/MS run; 5.3.2 Quantification run; 5.3.3 Quantification experiment; 5.3.4 Quantification project; 5.3.5 Planning quantification experiments; 5.4 Comparing quantification approaches/methods; 5.4.1 Accuracy; 5.4.2 Precision; 5.4.3 Repeatability and reproducibility 5.4.4 Dynamic range and linear dynamic range |
| Record Nr. | UNINA-9910831040903321 |
|
Eidhammer Ingvar
|
||
| Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.]
| Computational and statistical methods for protein quantification by mass spectrometry [[electronic resource] /] / Ingvar Eidhammer ... [et al.] |
| Autore | Eidhammer Ingvar |
| Pubbl/distr/stampa | Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 |
| Descrizione fisica | 1 online resource (356 p.) |
| Disciplina |
572.636
572/.636 |
| Altri autori (Persone) |
BarsnesHarald
EideGeir Egil MartensLennart |
| Soggetto topico |
Proteomics - Statistical methods
Mass spectrometry - Data processing |
| ISBN |
1-118-49404-0
1-299-18826-5 1-118-49378-8 1-118-49377-X |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational and Statistical Methods for Protein Quantification by Mass Spectrometry; Contents; Preface; Terminology; Acknowledgements; 1 Introduction; 1.1 The composition of an organism; 1.1.1 A simple model of an organism; 1.1.2 Composition of cells; 1.2 Homeostasis, physiology, and pathology; 1.3 Protein synthesis; 1.4 Site, sample, state, and environment; 1.5 Abundance and expression - protein and proteome profiles; 1.5.1 The protein dynamic range; 1.6 The importance of exact specification of sites and states; 1.6.1 Biological features; 1.6.2 Physiological and pathological features
1.6.3 Input features1.6.4 External features; 1.6.5 Activity features; 1.6.6 The cell cycle; 1.7 Relative and absolute quantification; 1.7.1 Relative quantification; 1.7.2 Absolute quantification; 1.8 In vivo and in vitro experiments; 1.9 Goals for quantitative protein experiments; 1.10 Exercises; 2 Correlations of mRNA and protein abundances; 2.1 Investigating the correlation; 2.2 Codon bias; 2.3 Main results from experiments; 2.4 The ideal case for mRNA-protein comparison; 2.5 Exploring correlation across genes; 2.6 Exploring correlation within one gene; 2.7 Correlation across subsets 2.8 Comparing mRNA and protein abundances across genes from two situations2.9 Exercises; 2.10 Bibliographic notes; 3 Protein level quantification; 3.1 Two-dimensional gels; 3.1.1 Comparing results from different experiments - DIGE; 3.2 Protein arrays; 3.2.1 Forward arrays; 3.2.2 Reverse arrays; 3.2.3 Detection of binding molecules; 3.2.4 Analysis of protein array readouts; 3.3 Western blotting; 3.4 ELISA - Enzyme-Linked Immunosorbent Assay; 3.5 Bibliographic notes; 4 Mass spectrometry and protein identification; 4.1 Mass spectrometry; 4.1.1 Peptide mass fingerprinting (PMF) 4.1.2 MS/MS - tandem MS4.1.3 Mass spectrometers; 4.2 Isotope composition of peptides; 4.2.1 Predicting the isotope intensity distribution; 4.2.2 Estimating the charge; 4.2.3 Revealing isotope patterns; 4.3 Presenting the intensities - the spectra; 4.4 Peak intensity calculation; 4.5 Peptide identification by MS/MS spectra; 4.5.1 Spectral comparison; 4.5.2 Sequential comparison; 4.5.3 Scoring; 4.5.4 Statistical significance; 4.6 The protein inference problem; 4.6.1 Determining maximal explanatory sets; 4.6.2 Determining minimal explanatory sets; 4.7 False discovery rate for the identifications 4.7.1 Constructing the decoy database4.7.2 Separate or composite search; 4.8 Exercises; 4.9 Bibliographic notes; 5 Protein quantification by mass spectrometry; 5.1 Situations, protein, and peptide variants; 5.1.1 Situation; 5.1.2 Protein variants - peptide variants; 5.2 Replicates; 5.3 Run - experiment - project; 5.3.1 LC-MS/MS run; 5.3.2 Quantification run; 5.3.3 Quantification experiment; 5.3.4 Quantification project; 5.3.5 Planning quantification experiments; 5.4 Comparing quantification approaches/methods; 5.4.1 Accuracy; 5.4.2 Precision; 5.4.3 Repeatability and reproducibility 5.4.4 Dynamic range and linear dynamic range |
| Record Nr. | UNINA-9910841586903321 |
|
Eidhammer Ingvar
|
||
| Chichester, West Sussex, U.K., : John Wiley & Sons Inc., 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Exploration and analysis of DNA microarray and other high dimensional data / / Dhammika Amaratunga, Javier Cabrera, Ziv Shkedy, authors
| Exploration and analysis of DNA microarray and other high dimensional data / / Dhammika Amaratunga, Javier Cabrera, Ziv Shkedy, authors |
| Autore | Amaratunga Dhammika <1956-> |
| Edizione | [Second edition.] |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : John Wiley & Sons, , 2014 |
| Descrizione fisica | 1 online resource (346 p.) |
| Disciplina | 572/.636 |
| Altri autori (Persone) |
CabreraJavier
ShkedyZiv |
| Collana | Wiley series in probability and statistics |
| Soggetto topico | Protein microarrays - Statistical methods |
| ISBN |
1-118-36450-3
1-118-36453-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cover; Title Page; Contents; Preface; Chapter 1 A Brief Introduction; 1.1 A Note on Exploratory Data Analysis; 1.2 Computing Considerations and Software; 1.3 A Brief Outline of the Book; 1.4 Data Sets and Case Studies; 1.4.1 The Golub Data; 1.4.2 The Mouse5 Data; 1.4.3 The Khan Data; 1.4.4 The Sialin Data; 1.4.5 The Behavioral Study Data; 1.4.6 The Spiked-In Data; 1.4.7 The APOAI Study; 1.4.8 The Breast Cancer Data; 1.4.9 Platinum Spike Data Set; 1.4.10 Human Epidermal Squamous Carcinoma Cell Line A431 Experiment; 1.4.11 Note: Public Repositories of Microarray Data; Chapter 2 Genomics Basics
2.1 Genes2.2 Deoxyribonucleic Acid; 2.3 Gene Expression; 2.4 Hybridization Assays and Other Laboratory Techniques; 2.5 The Human Genome; 2.6 Genome Variations and Their Consequences; 2.7 Genomics; 2.8 The Role of Genomics in Pharmaceutical Research and Clinical Practice; 2.9 Proteins; 2.10 Bioinformatics; Supplementary Reading; Chapter 3 Microarrays; 3.1 Types of Microarray Experiments; 3.1.1 Experiment Type 1: Tissue-Specific Gene Expression; 3.1.2 Experiment Type 2: Developmental Genetics; 3.1.3 Experiment Type 3: Genetic Diseases; 3.1.4 Experiment Type 4: Complex Diseases 3.1.5 Experiment Type 5: Pharmacological Agents3.1.6 Experiment Type 6: Plant Breeding; 3.1.7 Experiment Type 7: Environmental Monitoring; 3.2 A Very Simple Hypothetical Microarray Experiment; 3.3 A Typical Microarray Experiment; 3.3.1 Microarray Preparation; 3.3.2 Sample Preparation; 3.3.3 The Hybridization Step; 3.3.4 Scanning the Microarray; 3.3.5 Interpreting the Scanned Image; 3.4 Multichannel cDNA Microarrays; 3.5 Oligonucleotide Microarrays; 3.6 Bead-Based Arrays; 3.7 Confirmation of Microarray Results; Supplementary Reading and Electronic References Chapter 4 Processing the Scanned Image4.1 Converting the Scanned Image to the Spotted Image; 4.1.1 Gridding; 4.1.2 Segmentation; 4.1.3 Quantification; 4.2 Quality Assessment; 4.2.1 Visualizing the Spotted Image; 4.2.2 Numerical Evaluation of Array Quality; 4.2.3 Spatial Problems; 4.2.4 Spatial Randomness; 4.2.5 Quality Control of Arrays; 4.2.6 Assessment of Spot Quality; 4.3 Adjusting for Background; 4.3.1 Estimating the Background; 4.3.2 Adjusting for the Estimated Background; 4.4 Expression-Level Calculation for Two-Channel cDNA Microarrays 4.5 Expression-Level Calculation for Oligonucleotide Microarrays4.5.1 The Average Difference; 4.5.2 A Weighted Average Difference; 4.5.3 Perfect Matches Only; 4.5.4 Background Adjustment Approach; 4.5.5 Model-Based Approach; 4.5.6 Absent-Present Calls; Supplementary Reading; Software Notes; Chapter 5 Preprocessing Microarray Data; 5.1 Logarithmic Transformation; 5.2 Variance Stabilizing Transformations; 5.3 Sources of Bias; 5.4 Normalization; 5.5 Intensity-Dependent Normalization; 5.5.1 Smooth Function Normalization; 5.5.2 Quantile Normalization; 5.5.3 Stagewise Normalization 5.5.4 Normalization of Two-Channel Arrays |
| Record Nr. | UNINA-9910138960903321 |
|
Amaratunga Dhammika <1956->
|
||
| Hoboken, New Jersey : , : John Wiley & Sons, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Exploration and analysis of DNA microarray and other high dimensional data / / Dhammika Amaratunga, Javier Cabrera, Ziv Shkedy, authors
| Exploration and analysis of DNA microarray and other high dimensional data / / Dhammika Amaratunga, Javier Cabrera, Ziv Shkedy, authors |
| Autore | Amaratunga Dhammika <1956-> |
| Edizione | [Second edition.] |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : John Wiley & Sons, , 2014 |
| Descrizione fisica | 1 online resource (346 p.) |
| Disciplina | 572/.636 |
| Altri autori (Persone) |
CabreraJavier
ShkedyZiv |
| Collana | Wiley series in probability and statistics |
| Soggetto topico | Protein microarrays - Statistical methods |
| ISBN |
1-118-36450-3
1-118-36453-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cover; Title Page; Contents; Preface; Chapter 1 A Brief Introduction; 1.1 A Note on Exploratory Data Analysis; 1.2 Computing Considerations and Software; 1.3 A Brief Outline of the Book; 1.4 Data Sets and Case Studies; 1.4.1 The Golub Data; 1.4.2 The Mouse5 Data; 1.4.3 The Khan Data; 1.4.4 The Sialin Data; 1.4.5 The Behavioral Study Data; 1.4.6 The Spiked-In Data; 1.4.7 The APOAI Study; 1.4.8 The Breast Cancer Data; 1.4.9 Platinum Spike Data Set; 1.4.10 Human Epidermal Squamous Carcinoma Cell Line A431 Experiment; 1.4.11 Note: Public Repositories of Microarray Data; Chapter 2 Genomics Basics
2.1 Genes2.2 Deoxyribonucleic Acid; 2.3 Gene Expression; 2.4 Hybridization Assays and Other Laboratory Techniques; 2.5 The Human Genome; 2.6 Genome Variations and Their Consequences; 2.7 Genomics; 2.8 The Role of Genomics in Pharmaceutical Research and Clinical Practice; 2.9 Proteins; 2.10 Bioinformatics; Supplementary Reading; Chapter 3 Microarrays; 3.1 Types of Microarray Experiments; 3.1.1 Experiment Type 1: Tissue-Specific Gene Expression; 3.1.2 Experiment Type 2: Developmental Genetics; 3.1.3 Experiment Type 3: Genetic Diseases; 3.1.4 Experiment Type 4: Complex Diseases 3.1.5 Experiment Type 5: Pharmacological Agents3.1.6 Experiment Type 6: Plant Breeding; 3.1.7 Experiment Type 7: Environmental Monitoring; 3.2 A Very Simple Hypothetical Microarray Experiment; 3.3 A Typical Microarray Experiment; 3.3.1 Microarray Preparation; 3.3.2 Sample Preparation; 3.3.3 The Hybridization Step; 3.3.4 Scanning the Microarray; 3.3.5 Interpreting the Scanned Image; 3.4 Multichannel cDNA Microarrays; 3.5 Oligonucleotide Microarrays; 3.6 Bead-Based Arrays; 3.7 Confirmation of Microarray Results; Supplementary Reading and Electronic References Chapter 4 Processing the Scanned Image4.1 Converting the Scanned Image to the Spotted Image; 4.1.1 Gridding; 4.1.2 Segmentation; 4.1.3 Quantification; 4.2 Quality Assessment; 4.2.1 Visualizing the Spotted Image; 4.2.2 Numerical Evaluation of Array Quality; 4.2.3 Spatial Problems; 4.2.4 Spatial Randomness; 4.2.5 Quality Control of Arrays; 4.2.6 Assessment of Spot Quality; 4.3 Adjusting for Background; 4.3.1 Estimating the Background; 4.3.2 Adjusting for the Estimated Background; 4.4 Expression-Level Calculation for Two-Channel cDNA Microarrays 4.5 Expression-Level Calculation for Oligonucleotide Microarrays4.5.1 The Average Difference; 4.5.2 A Weighted Average Difference; 4.5.3 Perfect Matches Only; 4.5.4 Background Adjustment Approach; 4.5.5 Model-Based Approach; 4.5.6 Absent-Present Calls; Supplementary Reading; Software Notes; Chapter 5 Preprocessing Microarray Data; 5.1 Logarithmic Transformation; 5.2 Variance Stabilizing Transformations; 5.3 Sources of Bias; 5.4 Normalization; 5.5 Intensity-Dependent Normalization; 5.5.1 Smooth Function Normalization; 5.5.2 Quantile Normalization; 5.5.3 Stagewise Normalization 5.5.4 Normalization of Two-Channel Arrays |
| Record Nr. | UNINA-9910810663903321 |
|
Amaratunga Dhammika <1956->
|
||
| Hoboken, New Jersey : , : John Wiley & Sons, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.]
| Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.] |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Amsterdam ; ; Boston, : Academic Press, c2007 |
| Descrizione fisica | 1 online resource (915 pages) |
| Disciplina | 572/.636 |
| Altri autori (Persone) | CavanaghJohn <1963-> |
| Soggetto topico |
Proteins - Analysis
Nuclear magnetic resonance spectroscopy |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-96292-5
9786610962921 0-08-047103-X |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front cover; Title page; Copyright page; Preface; Preface to the First Edition; Acknowledgements; Table of Contents; 1 Classical NMR Spectroscopy; 1.1 Nuclear Magnetism; 1.2 The Bloch Equations; 1.3 The One-Pulse NMR Experiment; 1.4 Linewidth; 1.5 Chemical Shift; 1.6 Scalar Coupling and Limitations of the Bloch Equations; References; 2 Theoretical Description of NMR Spectroscopy; 2.1 Postulates of Quantum Mechanics; 2.2 The Density Matrix; 2.3 Pulses and Rotation Operators; 2.4 Quantum Mechanical NMR Spectroscopy; 2.5 Quantum Mechanics of Multispin Systems; 2.6 Coherence
2.7 Product Operator Formalism2.8 Averaging of the Spin Hamiltonians and Residual Interactions; References; 3 Experimental Aspects of NMR Spectroscopy; 3.1 NMR Instrumentation; 3.2 Data Acquisition; 3.3 Data Processing; 3.4 Pulse Techniques; 3.5 Spin Decoupling; 3.6 B0 Field Gradients; 3.7 Water Suppression Techniques; 3.8 One-Dimensional 1H NMR Spectroscopy; References; 4 Multidimensional NMR Spectroscopy; 4.1 Two-Dimensional NMR Spectroscopy; 4.2 Coherence Transfer and Mixing; 4.3 Coherence Selection, Phase Cycling, and Field Gradients; 4.4 Resolution and Sensitivity 4.5 Three- and Four-Dimensional NMR SpectroscopyReferences; 5 Relaxation and Dynamic Processes; 5.1 Introduction and Survey of Theoretical Approaches; 5.2 The Master Equation; 5.3 Spectral Density Functions; 5.4 Relaxation Mechanisms; 5.5 Nuclear Overhauser Effect; 5.6 Chemical Exchange Effects in NMR Spectroscopy; References; 6 Experimental 1H NMR Methods; 6.1 Assessment of the 1D 1H Spectrum; 6.2 COSY-Type Experiments; 6.3 Multiple-Quantum Filtered COSY; 6.4 Multiple-Quantum Spectroscopy; 6.5 TOCSY; 6.6 Cross-Relaxation NMR Experiments; 6.7 1H 3D Experiments; References 7 Heteronuclear NMR Experiments7.1 Heteronuclear Correlation NMR Spectroscopy; 7.2 Heteronuclear-Edited NMR Spectroscopy; 7.3 13C-13C Correlations: The HCCH-COSY and HCCH-TOCSY Experiments; 7.4 3D Triple-Resonance Experiments; 7.5 Measurement of Scalar Coupling Constants; 7.6 Measurement of Residual Dipolar Coupling Constants; References; 8 Experimental NMR Relaxation Methods; 8.1 Pulse Sequences and Experimental Methods; 8.2 Picosecond-Nanosecond Dynamics; 8.3 Microsecond-Second Dynamics; References; 9 Larger Proteins and Molecular Interactions; 9.1 Larger Proteins 9.2 Intermolecular Interactions9.3 Methods for Rapid Data Acquisition; References; 10 Sequential Assignment, Structure Determination, and Other Applications; 10.1 Resonance Assignment Strategies; 10.2 Three-Dimensional Solution Structures; 10.3 Conclusion; References; Table of Symbols; List of Figures; List of Tables; Suggested Reading; Biomolecular NMR Spectroscopy; NMR Spectroscopy; Quantum Mechanics; Index; Spin-1/2 Product Operator Equations; Table of Constants |
| Record Nr. | UNINA-9910458701603321 |
| Amsterdam ; ; Boston, : Academic Press, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.]
| Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.] |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Amsterdam ; ; Boston, : Academic Press, c2007 |
| Descrizione fisica | 1 online resource (915 pages) |
| Disciplina | 572/.636 |
| Altri autori (Persone) | CavanaghJohn <1963-> |
| Soggetto topico |
Proteins - Analysis
Nuclear magnetic resonance spectroscopy |
| ISBN |
1-280-96292-5
9786610962921 0-08-047103-X |
| Classificazione |
35.62
35.71 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front cover; Title page; Copyright page; Preface; Preface to the First Edition; Acknowledgements; Table of Contents; 1 Classical NMR Spectroscopy; 1.1 Nuclear Magnetism; 1.2 The Bloch Equations; 1.3 The One-Pulse NMR Experiment; 1.4 Linewidth; 1.5 Chemical Shift; 1.6 Scalar Coupling and Limitations of the Bloch Equations; References; 2 Theoretical Description of NMR Spectroscopy; 2.1 Postulates of Quantum Mechanics; 2.2 The Density Matrix; 2.3 Pulses and Rotation Operators; 2.4 Quantum Mechanical NMR Spectroscopy; 2.5 Quantum Mechanics of Multispin Systems; 2.6 Coherence
2.7 Product Operator Formalism2.8 Averaging of the Spin Hamiltonians and Residual Interactions; References; 3 Experimental Aspects of NMR Spectroscopy; 3.1 NMR Instrumentation; 3.2 Data Acquisition; 3.3 Data Processing; 3.4 Pulse Techniques; 3.5 Spin Decoupling; 3.6 B0 Field Gradients; 3.7 Water Suppression Techniques; 3.8 One-Dimensional 1H NMR Spectroscopy; References; 4 Multidimensional NMR Spectroscopy; 4.1 Two-Dimensional NMR Spectroscopy; 4.2 Coherence Transfer and Mixing; 4.3 Coherence Selection, Phase Cycling, and Field Gradients; 4.4 Resolution and Sensitivity 4.5 Three- and Four-Dimensional NMR SpectroscopyReferences; 5 Relaxation and Dynamic Processes; 5.1 Introduction and Survey of Theoretical Approaches; 5.2 The Master Equation; 5.3 Spectral Density Functions; 5.4 Relaxation Mechanisms; 5.5 Nuclear Overhauser Effect; 5.6 Chemical Exchange Effects in NMR Spectroscopy; References; 6 Experimental 1H NMR Methods; 6.1 Assessment of the 1D 1H Spectrum; 6.2 COSY-Type Experiments; 6.3 Multiple-Quantum Filtered COSY; 6.4 Multiple-Quantum Spectroscopy; 6.5 TOCSY; 6.6 Cross-Relaxation NMR Experiments; 6.7 1H 3D Experiments; References 7 Heteronuclear NMR Experiments7.1 Heteronuclear Correlation NMR Spectroscopy; 7.2 Heteronuclear-Edited NMR Spectroscopy; 7.3 13C-13C Correlations: The HCCH-COSY and HCCH-TOCSY Experiments; 7.4 3D Triple-Resonance Experiments; 7.5 Measurement of Scalar Coupling Constants; 7.6 Measurement of Residual Dipolar Coupling Constants; References; 8 Experimental NMR Relaxation Methods; 8.1 Pulse Sequences and Experimental Methods; 8.2 Picosecond-Nanosecond Dynamics; 8.3 Microsecond-Second Dynamics; References; 9 Larger Proteins and Molecular Interactions; 9.1 Larger Proteins 9.2 Intermolecular Interactions9.3 Methods for Rapid Data Acquisition; References; 10 Sequential Assignment, Structure Determination, and Other Applications; 10.1 Resonance Assignment Strategies; 10.2 Three-Dimensional Solution Structures; 10.3 Conclusion; References; Table of Symbols; List of Figures; List of Tables; Suggested Reading; Biomolecular NMR Spectroscopy; NMR Spectroscopy; Quantum Mechanics; Index; Spin-1/2 Product Operator Equations; Table of Constants |
| Record Nr. | UNINA-9910784645003321 |
| Amsterdam ; ; Boston, : Academic Press, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.]
| Protein NMR spectroscopy [[electronic resource] ] : principles and practice / / editors, John Cavanagh ... [et al.] |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Amsterdam ; ; Boston, : Academic Press, c2007 |
| Descrizione fisica | 1 online resource (915 pages) |
| Disciplina | 572/.636 |
| Altri autori (Persone) | CavanaghJohn <1963-> |
| Soggetto topico |
Proteins - Analysis
Nuclear magnetic resonance spectroscopy |
| ISBN |
1-280-96292-5
9786610962921 0-08-047103-X |
| Classificazione |
35.62
35.71 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front cover; Title page; Copyright page; Preface; Preface to the First Edition; Acknowledgements; Table of Contents; 1 Classical NMR Spectroscopy; 1.1 Nuclear Magnetism; 1.2 The Bloch Equations; 1.3 The One-Pulse NMR Experiment; 1.4 Linewidth; 1.5 Chemical Shift; 1.6 Scalar Coupling and Limitations of the Bloch Equations; References; 2 Theoretical Description of NMR Spectroscopy; 2.1 Postulates of Quantum Mechanics; 2.2 The Density Matrix; 2.3 Pulses and Rotation Operators; 2.4 Quantum Mechanical NMR Spectroscopy; 2.5 Quantum Mechanics of Multispin Systems; 2.6 Coherence
2.7 Product Operator Formalism2.8 Averaging of the Spin Hamiltonians and Residual Interactions; References; 3 Experimental Aspects of NMR Spectroscopy; 3.1 NMR Instrumentation; 3.2 Data Acquisition; 3.3 Data Processing; 3.4 Pulse Techniques; 3.5 Spin Decoupling; 3.6 B0 Field Gradients; 3.7 Water Suppression Techniques; 3.8 One-Dimensional 1H NMR Spectroscopy; References; 4 Multidimensional NMR Spectroscopy; 4.1 Two-Dimensional NMR Spectroscopy; 4.2 Coherence Transfer and Mixing; 4.3 Coherence Selection, Phase Cycling, and Field Gradients; 4.4 Resolution and Sensitivity 4.5 Three- and Four-Dimensional NMR SpectroscopyReferences; 5 Relaxation and Dynamic Processes; 5.1 Introduction and Survey of Theoretical Approaches; 5.2 The Master Equation; 5.3 Spectral Density Functions; 5.4 Relaxation Mechanisms; 5.5 Nuclear Overhauser Effect; 5.6 Chemical Exchange Effects in NMR Spectroscopy; References; 6 Experimental 1H NMR Methods; 6.1 Assessment of the 1D 1H Spectrum; 6.2 COSY-Type Experiments; 6.3 Multiple-Quantum Filtered COSY; 6.4 Multiple-Quantum Spectroscopy; 6.5 TOCSY; 6.6 Cross-Relaxation NMR Experiments; 6.7 1H 3D Experiments; References 7 Heteronuclear NMR Experiments7.1 Heteronuclear Correlation NMR Spectroscopy; 7.2 Heteronuclear-Edited NMR Spectroscopy; 7.3 13C-13C Correlations: The HCCH-COSY and HCCH-TOCSY Experiments; 7.4 3D Triple-Resonance Experiments; 7.5 Measurement of Scalar Coupling Constants; 7.6 Measurement of Residual Dipolar Coupling Constants; References; 8 Experimental NMR Relaxation Methods; 8.1 Pulse Sequences and Experimental Methods; 8.2 Picosecond-Nanosecond Dynamics; 8.3 Microsecond-Second Dynamics; References; 9 Larger Proteins and Molecular Interactions; 9.1 Larger Proteins 9.2 Intermolecular Interactions9.3 Methods for Rapid Data Acquisition; References; 10 Sequential Assignment, Structure Determination, and Other Applications; 10.1 Resonance Assignment Strategies; 10.2 Three-Dimensional Solution Structures; 10.3 Conclusion; References; Table of Symbols; List of Figures; List of Tables; Suggested Reading; Biomolecular NMR Spectroscopy; NMR Spectroscopy; Quantum Mechanics; Index; Spin-1/2 Product Operator Equations; Table of Constants |
| Record Nr. | UNINA-9910811454703321 |
| Amsterdam ; ; Boston, : Academic Press, c2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||