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Record Nr. |
UNINA9910144732103321 |
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Titolo |
Biophysical analysis of membrane proteins : investigating structure and function / / edited by Eva Pebay-Peyroula |
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Pubbl/distr/stampa |
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Weinheim, [Germany] : , : Wiley-VCH Verlag GmbH & Co. KGaA, , 2008 |
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©2008 |
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ISBN |
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1-282-78421-8 |
9786612784217 |
3-527-62122-9 |
3-527-62123-7 |
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Descrizione fisica |
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1 online resource (369 p.) |
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Disciplina |
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Soggetti |
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Membrane proteins - Structure-activity relationships |
Membrane proteins - Analysis |
Cell membranes - Physiology |
Physical biochemistry |
Electronic books. |
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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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Biophysical Analysis of Membrane Proteins; Contents; Preface; The Editor; List of Contributors; Part I Introduction; 1 High-Resolution Structures of Membrane Proteins: From X-Ray Crystallography to an Integrated Approach of Membranes; 1.1 Membranes: A Soft Medium?; 1.2 Current Knowledge on Membrane Protein Structures; 1.2.1 An Overview of the Protein Data Bank; 1.2.2 Protein Sources for Structural Studies; 1.2.3 The Diversity of Membrane Protein Topologies; 1.2.4 Genome Analyses; 1.3 X-Ray Crystallography; 1.3.1 Crystallization of Membrane Proteins; 1.3.2 General Aspects of Crystallography |
1.3.3 Determining the Phases Associated with Diffracted Waves1.3.4 Structure Determination of Membrane Proteins; 1.3.4.1 Crystal Quality; 1.3.4.2 Phase Determination; 1.3.4.3 Crystal Freezing; 1.4 Recent Examples; 1.4.1 Bacterial Rhodopsins; 1.4.2 ADP/ATP Carrier; 1.4.3 |
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Oligomerization of Membrane Proteins in their Natural Environment; 1.5 Future Developments in X-Ray Crystallography of Membrane Proteins; 1.6 Conclusions; Part II Structural Approaches; 2 Membrane Protein Structure Determination by Electron Cryo-Microscopy; 2.1 Introduction; 2.1.1 The Electron Microscope |
2.2 Single-Particle Electron Microscopy2.2.1 Sample Preparation and Requirements; 2.2.1.1 Negative Staining of Specimens; 2.2.1.2 Cryo-EM of Unstained Specimens; 2.2.1.3 Choice of detergent; 2.2.2 Image Analysis; 2.2.2.1 Classification of Images; 2.2.2.2 Model Building and Refinement; 2.2.2.3 Assessing Resolution; 2.2.3 Future Perspectives; 2.3 Structure Determination from 2-Dimensional Crystals; 2.3.1 Two-Dimensional Crystallization of Membrane Proteins; 2.3.2 Image Acquisition and Structure Determination; 2.3.3 Future Perspectives; 2.4 Helical Analysis of Tubes; 2.5 Conclusions |
3 Introduction to Solid-State NMR and its Application to Membrane Protein-Ligand Binding Studies3.1 Introduction; 3.1.1 Membrane Proteins: A Challenge; 3.1.2 Why Solid-State NMR?; 3.2 Solid-State NMR; 3.2.1 Sample Preparation: What is an Ideal Sample?; 3.2.1.1 Availability; 3.2.1.2 Stability; 3.2.1.3 Secondary Structure; 3.2.1.4 Sample Form: Local Order; 3.2.2 NMR Active Isotopes and Labeling; 3.2.3 Assignment and Structure Determination; 3.2.4 NMR Techniques: Solution- versus Solid-State NMR; 3.2.4.1 Isotropic Liquids; 3.2.4.2 Anisotropic Liquids; 3.2.4.3 Solids |
3.3 Examples: Receptor-Ligand Studies by Solid-State NMR3.3.1 Transport Proteins; 3.3.1.1 LacS; 3.3.2 G-Protein-Coupled Receptors and Related Proteins; 3.3.2.1 Bacteriorhodopsin, Rhodopsin, and Sensory Rhodopsin (NpSRII); 3.3.2.2 Human H(1) Receptor; 3.3.2.3 Neurotensin Receptor; 3.3.3 Ion Channels; 3.3.3.1 Nicotinic Acetylcholine Receptor; 3.3.3.2 K(+) Ion Channel, KcsA; 3.3.4 P-type ATPases; 3.3.5 Membrane Protein Soluble Alternatives; Part III Molecular Interaction and Large Assemblies; 4 Analytical Ultracentrifugation: Membrane Protein Assemblies in the Presence of Detergent |
4.1 Introduction |
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Sommario/riassunto |
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Meeting the need for a book on developing and using new methods to investigate membrane proteins, this is the first of its kind to present the full range of novel techniques in one resource. Top researchers from around the world focus on the physical principles exploited in the different techniques, and provide examples of how these can bring about important new insights.Following an introduction, further sections discuss structural approaches, molecular interaction and large assemblies, dynamics and spectroscopies, finishing off with an exploration of structure-function relationships in w |
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