NMR spectroscopy of biological solids. (2005)

• Record Type: Book
• Further Information: Note: Edited by A. Ramamoorthy.
• Other Names: Ramamoorthy, A (Ayyalusamy)
• Contents: COVER; Preface; Contributors; Table of Contents; 1; Magic-Angle Spinning Recoupling Techniques for Distance Determinations among Spin-1/2 Nuclei in Solid Peptides and Proteins; 1.1 Introduction; 1.2 Distance Measurements between Spin Pairs; 1.2.1 Sample Design and Experiment Goals; 1.2.2 Heteronuclear Recoupling by Rotational Echo Double Resonance; 1.2.2.1 The REDOR Concept; 1.2.2.2 Applications of REDOR to Spin Pairs; 1.2.3 Homonuclear Recoupling Experiments; 1.2.3.1 The Rotational Resonance Family (Zero Quantum Recoupling) 1.2.3.2 The Dipolar Recoupling at the Magic-Angle Family (Double Quantum Recoupling)1.2.4 Concluding Remarks about Spin-Pair Measurements; 1.3 The Spin Cluster Limit: A Few to a Dozen Spins; 1.3.1 Heteronuclear Experiments; 1.3.2 Homonuclear Experiments; 1.4 The Uniformly Labeled Limit: Dozens to Hundreds of Spins; 1.4.1 Sample Preparation and Chemical Shift Assignments; 1.4.2 Uniform and 100% Labeling; 1.4.3 Spin Dilution; 1.5 Conclusions and Prospects for High- Resolution Protein Structure Determination; Acknowledgments; References; 2 Spectral Assignment of (Membrane) Proteins under Magic-Angle Spinning2.1 Introduction; 2.2 Methods; 2.2.1 Spectral Resolution; 2.2.2 Polarization Transfer Schemes; 2.3 Applications; 2.3.1 Globular Proteins; 2.3.2 Protein Folding; 2.3.3 Membrane Peptides and Proteins; 2.4 Conclusions and Outlook; Acknowledgments; References; 3; Resonance Assignments and Secondary Structure Determination in Uniformly and Differentially Enriched Proteins and Protein Reassemblies by Magic- Angle Spinning Nuclear Magnetic Resonance Spectroscopy; 3.1 Introduction 3.2 Sample Preparation Strategies for High- Resolution Structural Studies of Proteins by MAS NMR Spectroscopy3.2.1 E. coli Thioredoxin: General Background; 3.2.2 Sample Morphology and Precipitation Conditions; 3.2.3 Differentially Enriched Thioredoxin Reassemblies for High-Resolution MAS Studies of Protein Interfaces; 3.3 Experimental Protocols for Resonance Assignments; 3.3.1 General Considerations; 3.3.2 Backbone Correlations; 3.3.3 Side-Chain Correlations; 3.3.4 Resonance Assignments in Reassembled Thioredoxin; 3.3.5 Resonance Assignments in Full-Length Intact Thioredoxin 3.4 Secondary Structure Determination3.5 Conclusions and Future Prospects; Acknowledgments; References; 4; Torsion Angle Determination in Biological Solids by Solid- State Nuclear Magnetic Resonance; 4.1 Static Tensor Correlation Techniques; 4.2 High-Resolution MAS Tensor Correlation Techniques; 4.2.1 HCCH Experiment; 4.2.2 HNCH Technique: f Angle Determination; 4.2.3 Multiple f, y, and c1 Angles by 3D HNCH Experiments; 4.2.4 NCCN Technique: y Angle Determination; 4.2.5 HCCN Technique: a-Helical y Angles; 4.2.6 OCCH Techniques: y Angle Determination
• Publisher Details: Boca Raton : CRC/Taylor & Francis Group
• Publication Date: 2005
• Extent: 1 online resource (353 pages), illustrations
• Subjects: 570/.28; Nuclear magnetic resonance spectroscopy; Biomolecules -- Analysis; Solids; NATURE -- Reference; SCIENCE -- Life Sciences -- General; SCIENCE -- Life Sciences -- Biology; Biomolecules -- Analysis; Nuclear magnetic resonance spectroscopy; Solids; Biomolecules -- Analysis; Nuclear magnetic resonance spectroscopy; Solids; Nuclear Magnetic Resonance, Biomolecular; Electronic books; Electronic books
• Languages: English
• ISBNs: 1420027611; 9781420027617; 9781574444964; 1574444964
• Related ISBNs: 1574444964
• Notes: Note: Includes bibliographical references and index.; Note: Print version record.
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.