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Frances Separovic & Akira Naito 
Advances in Biological Solid-State NMR 
Proteins and Membrane-Active Peptides

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Cover von Frances Separovic & Akira Naito: Advances in Biological Solid-State NMR (PDF)

The complexity and heterogeneity of biological systems has posed an immense challenge in recent years. An increasingly important tool for obtaining molecular and atomic scale information on a range of large biological molecules and cellular components is solid state NMR. This technique can address fascinating problems in structural biology, including the arrangement of supramolecular complexes and fibril formation in relation to molecular folding, misfolding and aggregation.


Advances in Biological NMR brings the reader up to date with chapters from international leaders of this growing field, covering the most recent developments in the methodology and applications of solid state NMR to studies of membrane interactions and molecular motions. A much needed discussion of membrane systems is detailed alongside important developments in in situ analysis.


Topics include applications to biological membranes, membrane active peptides, membrane proteins, protein assemblies and in-cell NMR. This exposition of an invaluable technique will interest those working in a range of related spectroscopic and biological fields. A basic introduction invites those interested to familiarise themselves with the basic mathematical and conceptual foundations of solid state NMR. A thorough and comprehensive discussion of this promising technique follows, which is essential reading for those working or studying at postgraduate level in this exciting field.

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Inhaltsverzeichnis

Introduction to Biological Solid-State NMR; Combining NMR Spectroscopic Measurements and Molecular Dynamics Simulations to Determine the Orientation of Amphipathic Peptides in Lipid Bilayers; 13C−13C Distance Measurements by Polarisation Transfer Matrix Analysis of 13C Spin Diffusion in Uniformly 13C-Labeled Molecular Complex under Magic Angle Spinning; Demonstration of the Equivalence of Solid-state NMR Orientational Constraints from Magnetic and Rotational Alignment of the Coat Protein in a Filamentous Bacteriophage; Membrane Protein Interactions; Magnetic liposomes and bicelles: new tools for membrane-peptides structural studies; Membranes and Their Lipids: A Molecular Insight into Their Organization and Function; Structural studies of small bioactive compounds interacting with membranes and proteins; Lipopolysaccharide Induces Raft Domain Expansion in a Cholesterol-Containing Membrane; Deuterium NMR of mixed lipid membranes; Membrane Interactions of Amphiphilic Peptides with Antimicrobial Potential: A Solid-State NMR Study; Investigations of the structure, topology and dynamics of membrane-associated polypeptides by solid-state NMR spectroscopy; NMR of Lipids and Lipid/Peptide Mixtures; NMR investigations of the structure and dynamics of antimicrobial peptides: The peptaibol alamethicin; Solid-state NMR studies of antimicrobial peptide interactions with specific lipid environments; Dynamic Structure Analysis of Peptides in Membranes by Solid-State NMR; Structural Dynamics of Retinal in Rhodopsin Activation Viewed by Solid-State 2H NMR Spectroscopy; Helical Membrane Protein Structure: Strategy for Success; Chemistry and Structure via Solid-State NMR; Photoactivated Structural Changes in Photoreceptor Membrane Proteins as Revealed by in situ Photoirradiation Solid-State NMR Spectroscopy; A Promising Prognosis for Solid-State NMR of Functional Membrane Protein Complexes; Structural Topologies of Phosphorylated and Non-phosphorylated Oligomeric Phospholamban in Lipid Membranes by Hybrid NMR Approach; Structural Insights from solid-state NMR into the Function of the Bacteriorhodopsin Photoreceptor Protein; 2H solid-state NMR study of peptide-membrane interactions in intact bacteria; Magic Angle Spinning NMR Spectroscopy for Resolving Structure and Mechanisms of Function of Membrane Protein Assemblies Involved in Photosynthetic Energy Conversio; Large protein complexes revealed by solution state NMR: G Proteins and G Protein-activated inwardly rectifying potassium ion channel (GIRK); NMR studies of small molecules interacting with amyloidogenic proteins; Solid-State NMR Studies of β-Amyloid Fibrils and Related Assemblies; Subject Index
Sprache Englisch ● Format PDF ● Seiten 608 ● ISBN 9781782627449 ● Dateigröße 21.8 MB ● Herausgeber Frances Separovic & Akira Naito ● Verlag Royal Society of Chemistry ● Ort Cambridge ● Land GB ● Erscheinungsjahr 2014 ● Ausgabe 1 ● herunterladbar 24 Monate ● Währung EUR ● ID 6600603 ● Kopierschutz Adobe DRM
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