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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 | ||
| ||
High - performance liquid chromatography of peptides and proteins : separation, analysis, and conformation / editors ColinT. Mant, Robert S. Hodges.
| High - performance liquid chromatography of peptides and proteins : separation, analysis, and conformation / editors ColinT. Mant, Robert S. Hodges. |
| Pubbl/distr/stampa | Boca Raton, : CRC Press Inc., 1991 |
| Descrizione fisica | 938 p. ; 26 cm |
| Disciplina |
574.192 45
572.636 |
| Soggetto non controllato |
Proteine
Biochimica analitica |
| ISBN | 0-8493-6549-X |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-990001776760403321 |
| Boca Raton, : CRC Press Inc., 1991 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
High throughput protein expression and purification : methods and protocols / edited by Sharon A. Doyle
| High throughput protein expression and purification : methods and protocols / edited by Sharon A. Doyle |
| Pubbl/distr/stampa | Totowa : Humana Press, 2009 |
| Descrizione fisica | XII, 322 p., [2] p. di tav. : ill. ; 27 cm |
| Disciplina | 572.636 |
| Collana | Methods in molecular biology |
| Soggetto topico | Proteine - Genetica |
| ISBN | 978-1-58829-879-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNISA-990003195530203316 |
| Totowa : Humana Press, 2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Principles of Protein X-ray Crystallography / / by Jan Drenth
| Principles of Protein X-ray Crystallography / / by Jan Drenth |
| Autore | Drenth Jan |
| Edizione | [2nd ed. 1999.] |
| Pubbl/distr/stampa | New York, NY : , : Springer New York : , : Imprint : Springer, , 1999 |
| Descrizione fisica | 1 online resource (XV, 341 p.) |
| Disciplina |
572
572.636 |
| Collana | Springer Advanced Texts in Chemistry |
| Soggetto topico |
Biochemistry
Analytical chemistry Biophysics Biological physics Biochemistry, general Analytical Chemistry Biological and Medical Physics, Biophysics |
| ISBN | 1-4757-3092-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | 1 Crystallizing a Protein -- 2 X-ray Sources and Detectors -- 3 Crystals -- 4 The Theory of X-ray Diffraction by a Crystal -- 5 Average Reflection Intensity and Distribution of Structure Factor Data -- 6 Special Forms of the Structure Factor -- 7 The Solution of the Phase Problem by the Isomorphous Replacement Method -- 8 Phase Improvement -- 9 Anomalous Scattering in the Determination of the Protein Phase Angles and the Absolute Configuration -- 10 Molecular Replacement -- 11 Direct Methods -- 12 Laue Diffraction -- 13 Refinement of the Model Structure -- 14 The Combination of Phase Information -- 15 Checking for Gross Errors and Estimating the Accuracy of the Structural Model -- Appendix 1 A Compilation of Equations for Calculating Electron Density Maps -- Appendix 2 A Compilation of Reliability Indices -- Appendix 3 The Variation in the Intensity of X-ray Radiation -- References. |
| Record Nr. | UNINA-9910823189103321 |
|
Drenth Jan
|
||
| New York, NY : , : Springer New York : , : Imprint : Springer, , 1999 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein microarray technology [[electronic resource] /] / edited by Dev Kambhampati
| Protein microarray technology [[electronic resource] /] / edited by Dev Kambhampati |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (277 p.) |
| Disciplina |
572.636
572.8636 |
| Altri autori (Persone) | KambhampatiDev |
| Soggetto topico |
Protein microarrays
Physiology |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-52030-2
9786610520305 3-527-60521-5 3-527-60155-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Microarray Technology; Preface; Contents; List of Authors; Colour Plates; 1 Protein Microarrays: From Fundamental Screening to Clinical Diagnostics; 1.1 Potential Need for Protein Microarrays; 1.1.1 Protein Therapeutics; 1.1.2 Clinical Diagnostics; 1.1.3 National Security; 1.2 Current Applications of Protein Microarrays; 1.3 Problems and Challenges; 1.3.1 Sample Preparation and Handling (Probe and Target); 1.3.2 Microarray Platform; 1.3.3 Detection Technologies; 1.3.4 Data Analysis; 1.4 Potential Solutions: Enabling Technologies and Advancements; References
2 Protein Microarray Surface Chemistry and Coupling Schemes2.1 Introduction; 2.1.1 Background and Current State of Biomolecule Libraries; 2.2 Microarray Based of Class Substrates; 2.2.1 Surface Modification; 2.2.2 Current State of Glass-Based Protein Microarrays; 2.3 Microarrays based of Gold Substrates; 2.3.1 Surface Modifications; 2.3.2 Current State of Gold-based Protein Microarrays; 2.4 Microarrays based on Polymer Substrates; 2.4.1 Surface Modifications; 2.5 Special Formats: Microfluidic Devices and Integrated Semiconductor Chips; 2.6 Chemical Immobilization Techniques for Proteins 2.6.1 Covalent Chemical Coupling2.6.2 Photochemical Cross-Coupling; 2.6.3 Tagged Proteins; 2.6.4 Site-Specific Immobilization of Antibodies; 2.7 Conclusions; References; 3 Optimization of a Protein Microarray Platform Based on a Small-molecule Chemical Affinity System; 3.1 Introduction; 3.2 Experimental; 3.2.1 Reagents and Materials; 3.2.2 Comparison of the Intrinsic Fluorescence and Non-Specific Protein Binding of 2-D and 3-D SHA-Coated Glass Slides; 3.2.2.1 Preparation of 2D SHA-Coated Glass Surfaces; 3.2.2.2 Preparation of PDBA-modified Bovine Serum Albumin 3.2.2.3 Preparation of PDBA-modified Human IgG3.2.2.4 Printing and Development of 2-D and 3-D SHA-coated Glass Slides; 3.2.2.5 Comparison of the Intrinsic Flurescence of Unmodified, 2-D and 3-D SHA-coated Glass Slides; 3.2.2.6 Determination of the Non-Specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.2.3 Immunoassay Using a 3-D SHA-coated Glass Slide; 3.2.3.1 Preparation of PDBA-Cy3-modified Bovine Serum Albumin, PDBA-Human IgG, PDBA-Goat anti Human IgG; 3.2.3.2 Printing the Array and Analyzing the Data 3.2.4 Stability of the PDBA-Protein Conjugates Immobilized on 3-D-SHA-coated Glass Slides3.2.4.1 Preparation of PDBA-modified Goat Anti-rabbit Fc-specific IgG, PDBA-modified Goat Anti-rabbit Fc-specific F(ab)(2), PDBA-modified Goat Anti-human F(ab)(2), and PDBA-modified Goat Anti-mouse Fcγ-specific F(ab)(2); 3.2.4.2 Printing and Reading the Array; 3.3 Results and Discussion; 3.3.1 Comparison of the Intrinsic Fluorescence and Non-specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.3.2 Immunoassay on a 3-D SHA-coated Slide 3.3.3 Stability of PDBA-Protein Conjugates Immobilized on 3-D SHA-coated Glass Slides |
| Record Nr. | UNINA-9910146239103321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein microarray technology [[electronic resource] /] / edited by Dev Kambhampati
| Protein microarray technology [[electronic resource] /] / edited by Dev Kambhampati |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (277 p.) |
| Disciplina |
572.636
572.8636 |
| Altri autori (Persone) | KambhampatiDev |
| Soggetto topico |
Protein microarrays
Physiology |
| ISBN |
1-280-52030-2
9786610520305 3-527-60521-5 3-527-60155-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Microarray Technology; Preface; Contents; List of Authors; Colour Plates; 1 Protein Microarrays: From Fundamental Screening to Clinical Diagnostics; 1.1 Potential Need for Protein Microarrays; 1.1.1 Protein Therapeutics; 1.1.2 Clinical Diagnostics; 1.1.3 National Security; 1.2 Current Applications of Protein Microarrays; 1.3 Problems and Challenges; 1.3.1 Sample Preparation and Handling (Probe and Target); 1.3.2 Microarray Platform; 1.3.3 Detection Technologies; 1.3.4 Data Analysis; 1.4 Potential Solutions: Enabling Technologies and Advancements; References
2 Protein Microarray Surface Chemistry and Coupling Schemes2.1 Introduction; 2.1.1 Background and Current State of Biomolecule Libraries; 2.2 Microarray Based of Class Substrates; 2.2.1 Surface Modification; 2.2.2 Current State of Glass-Based Protein Microarrays; 2.3 Microarrays based of Gold Substrates; 2.3.1 Surface Modifications; 2.3.2 Current State of Gold-based Protein Microarrays; 2.4 Microarrays based on Polymer Substrates; 2.4.1 Surface Modifications; 2.5 Special Formats: Microfluidic Devices and Integrated Semiconductor Chips; 2.6 Chemical Immobilization Techniques for Proteins 2.6.1 Covalent Chemical Coupling2.6.2 Photochemical Cross-Coupling; 2.6.3 Tagged Proteins; 2.6.4 Site-Specific Immobilization of Antibodies; 2.7 Conclusions; References; 3 Optimization of a Protein Microarray Platform Based on a Small-molecule Chemical Affinity System; 3.1 Introduction; 3.2 Experimental; 3.2.1 Reagents and Materials; 3.2.2 Comparison of the Intrinsic Fluorescence and Non-Specific Protein Binding of 2-D and 3-D SHA-Coated Glass Slides; 3.2.2.1 Preparation of 2D SHA-Coated Glass Surfaces; 3.2.2.2 Preparation of PDBA-modified Bovine Serum Albumin 3.2.2.3 Preparation of PDBA-modified Human IgG3.2.2.4 Printing and Development of 2-D and 3-D SHA-coated Glass Slides; 3.2.2.5 Comparison of the Intrinsic Flurescence of Unmodified, 2-D and 3-D SHA-coated Glass Slides; 3.2.2.6 Determination of the Non-Specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.2.3 Immunoassay Using a 3-D SHA-coated Glass Slide; 3.2.3.1 Preparation of PDBA-Cy3-modified Bovine Serum Albumin, PDBA-Human IgG, PDBA-Goat anti Human IgG; 3.2.3.2 Printing the Array and Analyzing the Data 3.2.4 Stability of the PDBA-Protein Conjugates Immobilized on 3-D-SHA-coated Glass Slides3.2.4.1 Preparation of PDBA-modified Goat Anti-rabbit Fc-specific IgG, PDBA-modified Goat Anti-rabbit Fc-specific F(ab)(2), PDBA-modified Goat Anti-human F(ab)(2), and PDBA-modified Goat Anti-mouse Fcγ-specific F(ab)(2); 3.2.4.2 Printing and Reading the Array; 3.3 Results and Discussion; 3.3.1 Comparison of the Intrinsic Fluorescence and Non-specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.3.2 Immunoassay on a 3-D SHA-coated Slide 3.3.3 Stability of PDBA-Protein Conjugates Immobilized on 3-D SHA-coated Glass Slides |
| Record Nr. | UNINA-9910831070703321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein microarray technology / / edited by Dev Kambhampati
| Protein microarray technology / / edited by Dev Kambhampati |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
| Descrizione fisica | 1 online resource (277 p.) |
| Disciplina |
572.636
572.8636 |
| Altri autori (Persone) | KambhampatiDev |
| Soggetto topico |
Protein microarrays
Physiology |
| ISBN |
1-280-52030-2
9786610520305 3-527-60521-5 3-527-60155-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein Microarray Technology; Preface; Contents; List of Authors; Colour Plates; 1 Protein Microarrays: From Fundamental Screening to Clinical Diagnostics; 1.1 Potential Need for Protein Microarrays; 1.1.1 Protein Therapeutics; 1.1.2 Clinical Diagnostics; 1.1.3 National Security; 1.2 Current Applications of Protein Microarrays; 1.3 Problems and Challenges; 1.3.1 Sample Preparation and Handling (Probe and Target); 1.3.2 Microarray Platform; 1.3.3 Detection Technologies; 1.3.4 Data Analysis; 1.4 Potential Solutions: Enabling Technologies and Advancements; References
2 Protein Microarray Surface Chemistry and Coupling Schemes2.1 Introduction; 2.1.1 Background and Current State of Biomolecule Libraries; 2.2 Microarray Based of Class Substrates; 2.2.1 Surface Modification; 2.2.2 Current State of Glass-Based Protein Microarrays; 2.3 Microarrays based of Gold Substrates; 2.3.1 Surface Modifications; 2.3.2 Current State of Gold-based Protein Microarrays; 2.4 Microarrays based on Polymer Substrates; 2.4.1 Surface Modifications; 2.5 Special Formats: Microfluidic Devices and Integrated Semiconductor Chips; 2.6 Chemical Immobilization Techniques for Proteins 2.6.1 Covalent Chemical Coupling2.6.2 Photochemical Cross-Coupling; 2.6.3 Tagged Proteins; 2.6.4 Site-Specific Immobilization of Antibodies; 2.7 Conclusions; References; 3 Optimization of a Protein Microarray Platform Based on a Small-molecule Chemical Affinity System; 3.1 Introduction; 3.2 Experimental; 3.2.1 Reagents and Materials; 3.2.2 Comparison of the Intrinsic Fluorescence and Non-Specific Protein Binding of 2-D and 3-D SHA-Coated Glass Slides; 3.2.2.1 Preparation of 2D SHA-Coated Glass Surfaces; 3.2.2.2 Preparation of PDBA-modified Bovine Serum Albumin 3.2.2.3 Preparation of PDBA-modified Human IgG3.2.2.4 Printing and Development of 2-D and 3-D SHA-coated Glass Slides; 3.2.2.5 Comparison of the Intrinsic Flurescence of Unmodified, 2-D and 3-D SHA-coated Glass Slides; 3.2.2.6 Determination of the Non-Specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.2.3 Immunoassay Using a 3-D SHA-coated Glass Slide; 3.2.3.1 Preparation of PDBA-Cy3-modified Bovine Serum Albumin, PDBA-Human IgG, PDBA-Goat anti Human IgG; 3.2.3.2 Printing the Array and Analyzing the Data 3.2.4 Stability of the PDBA-Protein Conjugates Immobilized on 3-D-SHA-coated Glass Slides3.2.4.1 Preparation of PDBA-modified Goat Anti-rabbit Fc-specific IgG, PDBA-modified Goat Anti-rabbit Fc-specific F(ab)(2), PDBA-modified Goat Anti-human F(ab)(2), and PDBA-modified Goat Anti-mouse Fcγ-specific F(ab)(2); 3.2.4.2 Printing and Reading the Array; 3.3 Results and Discussion; 3.3.1 Comparison of the Intrinsic Fluorescence and Non-specific Protein Binding of 2-D and 3-D SHA-coated Glass Slides; 3.3.2 Immunoassay on a 3-D SHA-coated Slide 3.3.3 Stability of PDBA-Protein Conjugates Immobilized on 3-D SHA-coated Glass Slides |
| Record Nr. | UNINA-9910841342403321 |
| Weinheim, : Wiley-VCH, c2004 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein NMR spectroscopy : principles and practice / John Cavanagh...[et al.]
| Protein NMR spectroscopy : principles and practice / John Cavanagh...[et al.] |
| Edizione | [2. ed.] |
| Pubbl/distr/stampa | Amsterdam [etc.] : Elsevier, copyr. 2007 |
| Descrizione fisica | XXV, 885 p. ; 23 cm |
| Disciplina | 572.636 |
| Soggetto topico |
Proteine - Analisi
Risonanza magnetica nucleare |
| ISBN | 978-0-12-164491-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNISA-990003145850203316 |
| Amsterdam [etc.] : Elsevier, copyr. 2007 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
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