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Record Nr. |
UNINA9910783388003321 |
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Autore |
Robbins Joel <1961-> |
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Titolo |
Becoming sinners [[electronic resource] ] : Christianity and moral torment in a Papua New Guinea society / / by Joel Robbins |
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Pubbl/distr/stampa |
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Berkeley, Calif., : University of California Press, c2004 |
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ISBN |
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9786612762888 |
1-282-76288-5 |
0-520-93708-2 |
1-59734-483-4 |
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Descrizione fisica |
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1 online resource (413 p.) |
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Collana |
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Ethnographic studies in subjectivity ; ; 4 |
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Disciplina |
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Soggetti |
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Christianity - Papua New Guinea - Urapmin |
Ethnography |
Urapmin (Papua New Guinea) Religious life and customs |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references (p. 351-376) and index. |
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Nota di contenuto |
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Part one : becoming sinners -- From salt to the law : contact and the early colonial period -- Christianity and the colonial transformation of regional relations -- Revival, second stage conversion, and the localization of the Urapmin Church -- Part two : living in sin -- Contemporary Urapmin in millennial time and space -- Willfulness, lawfulness, and Urapmin morality -- Desire and its discontents : free time and Christian morality -- Rituals of redemption and technologies of the self -- Millennialism and the contest of values -- Christianity, cultural change, and the moral life of the hybrid. |
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Sommario/riassunto |
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In a world of swift and sweeping cultural transformations, few have seen changes as rapid and dramatic as those experienced by the Urapmin of Papua New Guinea in the last four decades. A remote people never directly "missionized," the Urapmin began in the 1960's to send young men to study with Baptist missionaries living among neighboring communities. By the late 1970's, the Urapmin had undergone a charismatic revival, abandoning their traditional religion for a Christianity intensely focused on human sinfulness and driven by a constant sense of millennial expectation. Exploring the Christian |
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culture of the Urapmin, Joel Robbins shows how its preoccupations provide keys to understanding the nature of cultural change more generally. In so doing, he offers one of the richest available anthropological accounts of Christianity as a lived religion. Theoretically ambitious and engagingly written, his book opens a unique perspective on a Melanesian society, religious experience, and the very nature of rapid cultural change. |
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2. |
Record Nr. |
UNINA9910830762703321 |
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Autore |
Kaltashov Igor A. |
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Titolo |
Mass spectrometry in structural biology and biophysics : architecture, dynamics, and interaction of biomolecules / / Igor A. Kaltashov, Stephen J. Eyles |
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Pubbl/distr/stampa |
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Hoboken, New Jersey : , : Wiley, , 2012 |
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©2012 |
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ISBN |
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1-280-59028-9 |
9786613620118 |
1-118-23211-9 |
1-118-23212-7 |
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Edizione |
[2nd ed.] |
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Descrizione fisica |
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1 online resource (312 p.) |
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Collana |
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Wiley series on mass spectrometry |
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Disciplina |
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Soggetti |
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Mass spectrometry |
Biophysics |
Biomolecules - Spectra |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references at the end of each chapters and index. |
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Nota di contenuto |
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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 |
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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 |
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Sommario/riassunto |
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The definitive guide to mass spectrometry techniques in biology and biophysics The use of mass spectrometry (MS) to study the architecture and dynamics of proteins is increasingly common within the biophysical community, and Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition provides readers with detailed, systematic coverage of the current state of the art. Offering an unrivalled overview of modern MS-based armamentarium that can be used to solve the most challenging problems in biophysics, structural biol |
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