Info
- Utilizzare la checkbox di selezione a fianco di ciascun documento per attivare le funzionalità di stampa, invio email, download nei formati disponibili del (i) record.
Proteins in solution and at interfaces [[electronic resource] ] : methods and applications in biotechnology and materials science / / edited by Juan M. Ruso, Ángel Piñeiro
| Proteins in solution and at interfaces [[electronic resource] ] : methods and applications in biotechnology and materials science / / edited by Juan M. Ruso, Ángel Piñeiro |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons Inc., 2013 |
| Descrizione fisica | 1 online resource (518 p.) |
| Disciplina | 660.6/3 |
| Altri autori (Persone) |
RusoJuan M (Ruso Beiras, Juan Manuel)
PiñeiroÁngel <1973-> |
| Collana | Wiley series on surface and interfacial chemistry |
| Soggetto topico | Proteins - Biotechnology |
| ISBN |
1-118-52306-7
1-299-14787-9 1-118-52318-0 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEINS IN SOLUTION AND AT INTERFACES; CONTENTS; PREFACE; CONTRIBUTORS; PART I; 1 X-RAY CRYSTALLOGRAPHY OF BIOLOGICAL MACROMOLECULES: FUNDAMENTALS AND APPLICATIONS; 1.1 INTRODUCTION; 1.2 FUNDAMENTALS OF X-RAY DIFFRACTION; 1.2.1 X-Ray Radiation and Interaction with Matter; 1.2.2 Crystals and Symmetry; 1.2.3 Diffraction by Crystals; 1.2.4 Real and Reciprocal Space; 1.2.5 Structure Factors; 1.2.6 Fourier Synthesis and Transform; 1.2.7 The Phase Problem; 1.3 THE STRUCTURE DETERMINATION PROCESS; 1.3.1 Sample Production and Conditioning; 1.3.2 Crystallization; 1.3.3 Data Collection and Processing
1.3.4 Structure Determination1.3.5 Electron Density Map Interpretation: Model Construction; 1.3.6 Model Refinement; 1.3.7 Validation; 1.4 STRUCTURAL ANALYSIS AND BIOLOGICAL IMPLICATIONS; 1.4.1 Structural Analysis; 1.4.2 Biological Implications; 1.5 FUTURE PROSPECTS; ACKNOWLEDGMENTS; REFERENCES; 2 NUCLEAR MAGNETIC RESONANCE METHODS FOR STUDYING SOLUBLE, FIBROUS, AND MEMBRANE-EMBEDDED PROTEINS; 2.1 INTRODUCTION AND BACKGROUND; 2.1.1 Nuclear Angular Momentum; 2.1.2 Chemical Shifts; 2.1.3 Nuclear Spin Interactions; 2.1.4 Relaxation; 2.1.5 Isotopic Labeling; 2.1.6 Samples; 2.2 STRUCTURAL DATA 2.2.1 Resonance Assignment2.2.2 Distance Measurements; 2.2.3 Angular Information; 2.2.4 Residual Dipolar Couplings; 2.2.5 Use of Paramagnetic Agents; 2.2.6 Oriented Samples; 2.2.7 Structure Calculations; 2.3 DYNAMICS; 2.3.1 Fast (ps-ns) Motions; 2.3.2 Slow (μs-ms) Motions; 2.3.3 Motions in Solids; 2.4 INTERMOLECULAR INTERACTIONS; 2.4.1 Identification of Interaction Surfaces; 2.4.2 Structural Restraints; 2.5 DISCUSSION; 2.5.1 Large Protein Systems; 2.5.2 Advantages and Disadvantages of Solution and Solid-State MAS NMR; 2.5.3 Complementary Techniques; 2.6 CONCLUSION; REFERENCES 3 SMALL-ANGLE X-RAY SCATTERING APPLIED TO PROTEINS IN SOLUTION3.1 INTRODUCTION; 3.2 SAXS THEORY; 3.2.1 General Equations; 3.2.2 Isotropy; 3.2.3 Homogeneous Scattering Particles (Two-Phase Model); 3.2.4 Model-Independent Shape Analysis: Kratky's Representation, Guinier's Law, and Porod's Invariant; 3.2.5 Methods to Calculate P(q); 3.2.6 Protein-Protein Interaction: S(q) Evaluation; 3.3 EXAMPLES; 3.3.1 Rg, p(r), Kratky's Representation and Shape Reconstruction: Analysis of Protein TcOYE; 3.3.2 Guinier's Analysis and Multipole Expansion Shape Reconstruction: The Replication Factor C Case 3.3.3 Partial Folded and Unfolded Protein: Analysis of the Protein Bovine Serum Albumin, BSA, Under the Influence of Denaturing Agents3.4 PROTEIN INTERACTION: BSA CASE; 3.5 PROTEIN AGGREGATION; 3.6 CONCLUSION; ACKNOWLEDGMENTS; REFERENCES; 4 ANALYZING THE SOLUTION STATE OF PROTEIN STRUCTURE, INTERACTIONS, AND LIGANDS BY SPECTROSCOPIC METHODS; 4.1 INTRODUCTION; 4.1.1 Overview; 4.1.2 Protein Secondary Structures and Motifs; 4.1.3 Structure Determination: Spectroscopic Methods; 4.2 ULTRAVIOLET-VISIBLE ABSORPTION SPECTROSCOPY; 4.2.1 Background 4.2.2 Lambert-Beer Law: Determination of Protein Concentration |
| Record Nr. | UNINA-9910141511403321 |
| Hoboken, N.J., : John Wiley & Sons Inc., 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteins in solution and at interfaces : methods and applications in biotechnology and materials science / / edited by Juan M. Ruso, Ángel Piñeiro
| Proteins in solution and at interfaces : methods and applications in biotechnology and materials science / / edited by Juan M. Ruso, Ángel Piñeiro |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons Inc., 2013 |
| Descrizione fisica | 1 online resource (518 p.) |
| Disciplina | 660.6/3 |
| Altri autori (Persone) |
RusoJuan M (Ruso Beiras, Juan Manuel)
PiñeiroÁngel <1973-> |
| Collana | Wiley series on surface and interfacial chemistry |
| Soggetto topico | Proteins - Biotechnology |
| ISBN |
1-118-52306-7
1-299-14787-9 1-118-52318-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEINS IN SOLUTION AND AT INTERFACES; CONTENTS; PREFACE; CONTRIBUTORS; PART I; 1 X-RAY CRYSTALLOGRAPHY OF BIOLOGICAL MACROMOLECULES: FUNDAMENTALS AND APPLICATIONS; 1.1 INTRODUCTION; 1.2 FUNDAMENTALS OF X-RAY DIFFRACTION; 1.2.1 X-Ray Radiation and Interaction with Matter; 1.2.2 Crystals and Symmetry; 1.2.3 Diffraction by Crystals; 1.2.4 Real and Reciprocal Space; 1.2.5 Structure Factors; 1.2.6 Fourier Synthesis and Transform; 1.2.7 The Phase Problem; 1.3 THE STRUCTURE DETERMINATION PROCESS; 1.3.1 Sample Production and Conditioning; 1.3.2 Crystallization; 1.3.3 Data Collection and Processing
1.3.4 Structure Determination1.3.5 Electron Density Map Interpretation: Model Construction; 1.3.6 Model Refinement; 1.3.7 Validation; 1.4 STRUCTURAL ANALYSIS AND BIOLOGICAL IMPLICATIONS; 1.4.1 Structural Analysis; 1.4.2 Biological Implications; 1.5 FUTURE PROSPECTS; ACKNOWLEDGMENTS; REFERENCES; 2 NUCLEAR MAGNETIC RESONANCE METHODS FOR STUDYING SOLUBLE, FIBROUS, AND MEMBRANE-EMBEDDED PROTEINS; 2.1 INTRODUCTION AND BACKGROUND; 2.1.1 Nuclear Angular Momentum; 2.1.2 Chemical Shifts; 2.1.3 Nuclear Spin Interactions; 2.1.4 Relaxation; 2.1.5 Isotopic Labeling; 2.1.6 Samples; 2.2 STRUCTURAL DATA 2.2.1 Resonance Assignment2.2.2 Distance Measurements; 2.2.3 Angular Information; 2.2.4 Residual Dipolar Couplings; 2.2.5 Use of Paramagnetic Agents; 2.2.6 Oriented Samples; 2.2.7 Structure Calculations; 2.3 DYNAMICS; 2.3.1 Fast (ps-ns) Motions; 2.3.2 Slow (μs-ms) Motions; 2.3.3 Motions in Solids; 2.4 INTERMOLECULAR INTERACTIONS; 2.4.1 Identification of Interaction Surfaces; 2.4.2 Structural Restraints; 2.5 DISCUSSION; 2.5.1 Large Protein Systems; 2.5.2 Advantages and Disadvantages of Solution and Solid-State MAS NMR; 2.5.3 Complementary Techniques; 2.6 CONCLUSION; REFERENCES 3 SMALL-ANGLE X-RAY SCATTERING APPLIED TO PROTEINS IN SOLUTION3.1 INTRODUCTION; 3.2 SAXS THEORY; 3.2.1 General Equations; 3.2.2 Isotropy; 3.2.3 Homogeneous Scattering Particles (Two-Phase Model); 3.2.4 Model-Independent Shape Analysis: Kratky's Representation, Guinier's Law, and Porod's Invariant; 3.2.5 Methods to Calculate P(q); 3.2.6 Protein-Protein Interaction: S(q) Evaluation; 3.3 EXAMPLES; 3.3.1 Rg, p(r), Kratky's Representation and Shape Reconstruction: Analysis of Protein TcOYE; 3.3.2 Guinier's Analysis and Multipole Expansion Shape Reconstruction: The Replication Factor C Case 3.3.3 Partial Folded and Unfolded Protein: Analysis of the Protein Bovine Serum Albumin, BSA, Under the Influence of Denaturing Agents3.4 PROTEIN INTERACTION: BSA CASE; 3.5 PROTEIN AGGREGATION; 3.6 CONCLUSION; ACKNOWLEDGMENTS; REFERENCES; 4 ANALYZING THE SOLUTION STATE OF PROTEIN STRUCTURE, INTERACTIONS, AND LIGANDS BY SPECTROSCOPIC METHODS; 4.1 INTRODUCTION; 4.1.1 Overview; 4.1.2 Protein Secondary Structures and Motifs; 4.1.3 Structure Determination: Spectroscopic Methods; 4.2 ULTRAVIOLET-VISIBLE ABSORPTION SPECTROSCOPY; 4.2.1 Background 4.2.2 Lambert-Beer Law: Determination of Protein Concentration |
| Record Nr. | UNINA-9910817602803321 |
| Hoboken, N.J., : John Wiley & Sons Inc., 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||