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Mass spectrometry in structural biology and biophysics : architecture, dynamics, and interaction of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles
| Mass spectrometry in structural biology and biophysics : architecture, dynamics, and interaction of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles |
| Autore | Kaltashov Igor A. |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , 2012 |
| Descrizione fisica | 1 online resource (312 p.) |
| Disciplina |
610.28/4
610.284 |
| Collana | Wiley series on mass spectrometry |
| Soggetto topico |
Mass spectrometry
Biophysics Biomolecules - Spectra |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-59028-9
9786613620118 1-118-23211-9 1-118-23212-7 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
MASS SPECTROMETRY IN STRUCTURAL BIOLOGY AND BIOPHYSICS: Architecture, Dynamics, and Interaction of Biomolecules; CONTENTS; Preface to the Second Edition; Preface to the First Edition; 1 General Overview of Basic Concepts in Molecular Biophysics; 1.1 Covalent Structure of Biopolymers; 1.2 Noncovalent Interactions and Higher Order Structure; 1.2.1 Electrostatic Interaction; 1.2.2 Hydrogen Bonding; 1.2.3 Steric Clashes and Allowed Conformations of the Peptide Backbone: Secondary Structure; 1.2.4 Solvent--Solute Interactions, Hydrophobic Effect, Side-Chain Packing, and Tertiary Structure
1.2.5 Intermolecular Interactions and Association: Quaternary Structure1.3 The Protein Folding Problem; 1.3.1 What Is Protein Folding?; 1.3.2 Why Is Protein Folding So Important?; 1.3.3 What Is the Natively Folded Protein and How Do We Define a Protein Conformation?; 1.3.4 What Are Non-Native Protein Conformations?: Random Coils, Molten Globules, and Folding Intermediates; 1.3.5 Protein Folding Pathways; 1.4 Protein Energy Landscapes and the Folding Problem; 1.4.1 Protein Conformational Ensembles and Energy Landscapes: Enthalpic and Entropic Considerations 1.4.2 Equilibrium and Kinetic Intermediates on the Energy Landscape1.5 Protein Dynamics and Function; 1.5.1 Limitations of the Structure--Function Paradigm; 1.5.2 Protein Dynamics under Native Conditions; 1.5.3 Is Well-Defined Structure Required for Functional Competence?; 1.5.4 Biomolecular Dynamics and Binding from The Energy Landscape Perspective; 1.5.5 Energy Landscapes Within a Broader Context of Nonlinear Dynamics: Information Flow and Fitness Landscapes; 1.6 Protein Higher Order Structure and Dynamics from A Biotechnology Perspective; References 2 Overview of Traditional Experimental Arsenal to Study Biomolecular Structure and Dynamics2.1 X-Ray Crystallography; 2.1.1 Fundamentals; 2.1.2 Crystal Structures at Atomic and Ultrahigh Resolution; 2.1.3 Crystal Structures of Membrane Proteins; 2.1.4 Protein Dynamics and X-Ray Diffraction; 2.2 Solution Scattering Techniques; 2.2.1 Static and Dynamic Light Scattering; 2.2.2 Small-Angle X-Ray Scattering; 2.2.3 Cryo-Electron Microscopy; 2.2.4 Neutron Scattering; 2.3 NMR Spectroscopy; 2.3.1 Heteronuclear NMR; 2.3.2 Hydrogen Exchange by NMR; 2.4 Other Spectroscopic Techniques 2.4.1 Cumulative Measurements of Higher Order Structure: Circular Dichroism2.4.2 Vibrational Spectroscopy; 2.4.3 Fluorescence: Monitoring Specific Dynamic Events; 2.5 Other Biophysical Methods to Study Macromolecular Interactions and Dynamics; 2.5.1 Calorimetric Methods; 2.5.2 Analytical Ultracentrifugation; 2.5.3 Surface Plasmon Resonance; 2.5.4 Size Exclusion Chromatography (Gel Filtration); 2.5.5 Electrophoresis; 2.5.6 Affinity Chromatography; References; 3 Overview of Biological Mass Spectrometry; 3.1 Basic Principles of Mass Spectrometry; 3.1.1 Stable Isotopes and Isotopic Distributions 3.1.2 Macromolecular Mass: Terms and Definitions |
| Record Nr. | UNINA-9910141330003321 |
Kaltashov Igor A.
|
||
| Hoboken, New Jersey : , : Wiley, , 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Mass spectrometry in structural biology and biophysics : architecture, dynamics, and interaction of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles
| Mass spectrometry in structural biology and biophysics : architecture, dynamics, and interaction of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles |
| Autore | Kaltashov Igor A. |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , 2012 |
| Descrizione fisica | 1 online resource (312 p.) |
| Disciplina |
610.28/4
610.284 |
| Collana | Wiley series on mass spectrometry |
| Soggetto topico |
Mass spectrometry
Biophysics Biomolecules - Spectra |
| ISBN |
1-280-59028-9
9786613620118 1-118-23211-9 1-118-23212-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
MASS SPECTROMETRY IN STRUCTURAL BIOLOGY AND BIOPHYSICS: Architecture, Dynamics, and Interaction of Biomolecules; CONTENTS; Preface to the Second Edition; Preface to the First Edition; 1 General Overview of Basic Concepts in Molecular Biophysics; 1.1 Covalent Structure of Biopolymers; 1.2 Noncovalent Interactions and Higher Order Structure; 1.2.1 Electrostatic Interaction; 1.2.2 Hydrogen Bonding; 1.2.3 Steric Clashes and Allowed Conformations of the Peptide Backbone: Secondary Structure; 1.2.4 Solvent--Solute Interactions, Hydrophobic Effect, Side-Chain Packing, and Tertiary Structure
1.2.5 Intermolecular Interactions and Association: Quaternary Structure1.3 The Protein Folding Problem; 1.3.1 What Is Protein Folding?; 1.3.2 Why Is Protein Folding So Important?; 1.3.3 What Is the Natively Folded Protein and How Do We Define a Protein Conformation?; 1.3.4 What Are Non-Native Protein Conformations?: Random Coils, Molten Globules, and Folding Intermediates; 1.3.5 Protein Folding Pathways; 1.4 Protein Energy Landscapes and the Folding Problem; 1.4.1 Protein Conformational Ensembles and Energy Landscapes: Enthalpic and Entropic Considerations 1.4.2 Equilibrium and Kinetic Intermediates on the Energy Landscape1.5 Protein Dynamics and Function; 1.5.1 Limitations of the Structure--Function Paradigm; 1.5.2 Protein Dynamics under Native Conditions; 1.5.3 Is Well-Defined Structure Required for Functional Competence?; 1.5.4 Biomolecular Dynamics and Binding from The Energy Landscape Perspective; 1.5.5 Energy Landscapes Within a Broader Context of Nonlinear Dynamics: Information Flow and Fitness Landscapes; 1.6 Protein Higher Order Structure and Dynamics from A Biotechnology Perspective; References 2 Overview of Traditional Experimental Arsenal to Study Biomolecular Structure and Dynamics2.1 X-Ray Crystallography; 2.1.1 Fundamentals; 2.1.2 Crystal Structures at Atomic and Ultrahigh Resolution; 2.1.3 Crystal Structures of Membrane Proteins; 2.1.4 Protein Dynamics and X-Ray Diffraction; 2.2 Solution Scattering Techniques; 2.2.1 Static and Dynamic Light Scattering; 2.2.2 Small-Angle X-Ray Scattering; 2.2.3 Cryo-Electron Microscopy; 2.2.4 Neutron Scattering; 2.3 NMR Spectroscopy; 2.3.1 Heteronuclear NMR; 2.3.2 Hydrogen Exchange by NMR; 2.4 Other Spectroscopic Techniques 2.4.1 Cumulative Measurements of Higher Order Structure: Circular Dichroism2.4.2 Vibrational Spectroscopy; 2.4.3 Fluorescence: Monitoring Specific Dynamic Events; 2.5 Other Biophysical Methods to Study Macromolecular Interactions and Dynamics; 2.5.1 Calorimetric Methods; 2.5.2 Analytical Ultracentrifugation; 2.5.3 Surface Plasmon Resonance; 2.5.4 Size Exclusion Chromatography (Gel Filtration); 2.5.5 Electrophoresis; 2.5.6 Affinity Chromatography; References; 3 Overview of Biological Mass Spectrometry; 3.1 Basic Principles of Mass Spectrometry; 3.1.1 Stable Isotopes and Isotopic Distributions 3.1.2 Macromolecular Mass: Terms and Definitions |
| Record Nr. | UNINA-9910830762703321 |
|
Kaltashov Igor A.
|
||
| Hoboken, New Jersey : , : Wiley, , 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||