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[null,"1.","Record Nr.",null,"UNINA9910502201103321"]
[null,null,"Autore",null,"Fornasari, Gabriele"]
[null,null,"Titolo",null,"Dilemma etico del male minore e ticking bomb scenario : riflessioni penalistiche (e non) sulle strategie di legittimazione della tortura / Gabriele Fornasari"]
[null,null,"Pubbl/distr/stampa",null,"Napoli, : Edizioni scientifiche italiane, 2020"]
[null,null,"ISBN",null,"978-88-495-4434-3"]
[null,null,"Descrizione fisica",null,"293 p. ; 24 cm"]
[null,null,"Collana",null,"Fonti e studi per il diritto penale ; 4"]
[null,null,"Disciplina",null,"364.675"]
[null,null,"Locazione",null,"FSPBC"]
[null,null,"Collocazione",null,"COLLEZ. 2999 (4)"]
[null,null,"Lingua di pubblicazione",null,"Italiano"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Nota di bibliografia","Contiene bibl. (pp. 257-293)"]
[null,"2.","Record Nr.",null,"UNINA9910143577603321"]
[null,null,"Autore",null,"Kaltashov Igor A"]
[null,null,"Titolo",null,"Mass spectrometry in biophysics [[electronic resource] ] : conformation and dynamics of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles"]
[null,null,"Pubbl/distr/stampa",null,"Hoboken, N.J., : John Wiley, 2005"]
[null,null,"ISBN",null,"1-280-27538-3"]
[{"$nulls":4},"9786610275380"]
[{"$nulls":4},"0-470-24511-5"]
[{"$nulls":4},"0-471-70517-9"]
[{"$nulls":4},"0-471-70516-0"]
[null,null,"Descrizione fisica",null,"1 online resource (480 p.)"]
[null,null,"Collana",null,"Wiley-Interscience series on mass spectrometry"]
[null,null,"Disciplina",null,"572.33"]
[{"$nulls":4},"572.8"]
[{"$nulls":4},"572/.33"]
[null,null,"Soggetti",null,"Mass spectrometry"]
[{"$nulls":4},"Biophysics"]
[{"$nulls":4},"Biomolecules - Spectra"]
[{"$nulls":4},"Electronic books."]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Note generali","Description based upon print version of record."]
[null,null,null,"Nota di bibliografia","Includes bibliographical references and index."]
[null,null,"Nota di contenuto",null,"MASS SPECTROMETRY IN BIOPHYSICS; CONTENTS; Preface; 1 General Overview of Basic Concepts in Molecular Biophysics; 1.1. Covalent Structure of Biopolymers; 1.2. Noncovalent Interactions and Higher-order Structure; 1.2.1. Electrostatic Interaction; 1.2.2. Hydrogen Bonding; 1.2.3. Steric Clashes and Allowed Conformations of the Peptide Backbone: Secondary Structure; 1.2.4. Solvent-Solute Interactions, Hydrophobic Effect, Side Chain Packing, and Tertiary Structure; 1.2.5. Intermolecular Interactions and Association: Quaternary Structure; 1.3. The Protein Folding Problem"]
[{"$nulls":4},"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 "]
[{"$nulls":4},"Considerations; 1.4.2. Equilibrium and Kinetic Intermediates on the Energy Landscape; 1.5. Protein Dynamics and Function"]
[{"$nulls":4},"1.5.1. Limitations of the Structure-Function Paradigm1.5.2. Protein Dynamics Under Native Conditions; 1.5.3. Biomolecular Dynamics and Binding from the Energy Landscape Perspective; 1.5.4. Energy Landscapes Within a Broader Context of Nonlinear Dynamics: Information Flow and Fitness Landscapes; References; 2 Overview of \"Traditional\" Experimental Arsenal to Study Biomolecular Structure and Dynamics; 2.1. 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"]
[{"$nulls":4},"2.1.4. Protein Dynamics and X-Ray Diffraction2.2. Solution Scattering Techniques; 2.2.1. Static and Dynamic Light Scattering; 2.2.2. Small-Angle X-Ray Scattering; 2.2.3. Cryo-Electron Microscopy; 2.2.4. Neutron Scattering; 2.3. NMR Spectroscopy; 2.3.1. Heteronuclear NMR; 2.3.2. Hydrogen Exchange by NMR; 2.4. Other Spectroscopic Techniques; 2.4.1. Cumulative Measurements of Higher Order Structure: Circular Dichroism; 2.4.2. Vibrational Spectroscopy; 2.4.3. Fluorescence: Monitoring Specific Dynamic Events; 2.5. Other Biophysical Methods to Study Macromolecular Interactions and Dynamics"]
[{"$nulls":4},"2.5.1. Calorimetric Methods2.5.2. Analytical Ultracentrifugation; 2.5.3. Surface Plasmon Resonance; 2.5.4. Gel Filtration; 2.5.5. Gel Electrophoresis; 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; 3.2. Methods of Producing Biomolecular Ions; 3.2.1. Macromolecular Ion Desorption Techniques: General Considerations; 3.2.2. Electrospray Ionization; 3.2.3. Matrix Assisted Laser Desorption/Ionization; 3.3. Mass Analysis"]
[{"$nulls":4},"3.3.1. General Considerations: m/z Range and Mass Discrimination, Mass Resolution, Duty Cycle, Data Acquisition Rate"]
[null,null,null,"Sommario/riassunto","The first systematic summary of biophysical mass spectrometry techniquesRecent advances in mass spectrometry (MS) have pushed the frontiers of analytical chemistry into the biophysical laboratory. As a result, the biophysical community's acceptance of MS-based methods, used to study protein higher-order structure and dynamics, has accelerated the expansion of biophysical MS.Despite this growing trend, until now no single text has presented the full array of MS-based experimental techniques and strategies for biophysics. Mass Spectrometry in Biophysics expertly closes this gap i"]