Name: Biological Magnetic Resonance By Lawrence J. Berliner
SKU: 9781461565512
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Biological Magnetic Resonance Summary

Biological Magnetic Resonance by Lawrence J. Berliner

We are pleased to present Volume 9 of our highly successful series, which now celebrates 12 years of providing the magnetic resonance community with topical, authoritative chapters on new aspects of biological magnetic resonance. As always, we try to present a diversity of topic coverage in each volume, ranging from applications of in vivo magnetic resonance to more fundamental aspects of electron spin resonance and nuclear magnetic resonance. Philip Yeagle presents an eagerly awaited chapter on 31p NMR studies of membranes and membrane protein interactions. Alan Marshall has con tributed two chapters to the volume: one, with Jiejun Wu, describes magnetic resonance studies of 5S-RNA as probes of its structure and conformation; the secon

About Lawrence J. Berliner

Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He is the Series Editor for Biological Magnetic Resonance, which he launched in 1979.

1 Phosphorus NMR of Membranes.- 1. Introduction.- 1.1. Model and Biological Membrane Structures.- 1.2. 31P NMR of Membranes-Theoretical and Practical Aspects.- 2. 31P NMR and Membrane Morphology.- 2.1. Introduction.- 2.2. Model Membranes.- 2.3. Biological Membranes.- 3. 31P NMR and Membrane Structure and Dynamics.- 3.1. Phospholipid Headgroup Conformation.- 3.2. Phospholipid Headgroup Dynamics.- 3.3. Phospholipid-Protein Interactions.- 3.4. Transmembrane Phospholipid Distribution.- 4. New Areas for Investigation with 31P NMR.- References.- 2 Investigation of Ribosomal 5S Ribonucleic Acid Solution Structure and Dynamics by Means of High-Resolution Nuclear Magnetic Resonance Spectroscopy.- 1. Introduction.- 1.1. Non-NMR Methods.- 1.2. NMR Methods.- 2. NMR Strategies for RNA Solution Structure Determination.- 2.1. Proton FT-NMR in 1H2O.- 2.2. Adjunct Experiments for Assignment of Proton Resonances.- 2.3. Nuclei Other than Protons.- 3. Structural Analysis of Specific 5S rRNAs.- 3.1. E. Coli 5S rRNA and Its Enzyme-Cleaved Fragments.- 3.2. B. subtilis 5S rRNA.- 3.3. Wheat Germ 5S rRNA and Its Enzyme-Cleaved Fragments.- 3.4. Yeast 5S rRNA and Its Enzyme-Cleaved Fragments.- 3.5. Other 5S rRNAs.- 3.6. Yeast 5.8S rRNA.- 4. NMR Analysis of rRNA Structural Dynamics.- 4.1. Base-Pair Proton Exchange with Solvent.- 4.2. Heat-Induced Melting.- 4.3. Effects of Added Cations (Especially Mg2+).- 5. Conclusion and Perspectives for Future Work.- 5.1. Sequence Variation.- 5.2. Ribosomal Protein-RNA Interactions.- 5.3. Two-Dimensional Proton FT-NMR.- References.- 3 Structure Determination via Complete Relaxation Matrix Analysis (CORMA) of Two-Dimensional Nuclear Overhauser Effect Spectra: DNA Fragments.- 1. Introduction.- 2. Structure Evaluation Based on 2D NOE Spectroscopy.- 2.1. Basic 2D NOE Experiment: 90 Degrees - t1 - 90 Degrees - ?m - 90 Degrees - t2.- 2.2. Complete Relaxation Matrix Analysis-CORMA.- 2.3. Structure Evaluation by CORMA.- 2.4. Direct Determination of Distances by CORMA.- 2.5. Refinement of Structures Based on CORMA.- 3. Experimental Details of 2D NOE Spectroscopy.- 3.1. Special Techniques.- 3.2. Resonance Assignment.- 3.3. Intensity Measurement.- 4. Detailed Molecular Structure from 2D NOE Intensities.- References.- 4 Methods of Proton Resonance Assignment for Proteins.- 1. Introduction.- 1.1. Features of the Proton NMR Spectrum of a Protein.- 1.2. Proton NMR Assignments in Proteins.- 2. Protein Requirements.- 3. Instrumental Requirements.- 4. Sequential Assignments.- 4.1. Amino Acid Spin System Identification.- 4.2. Sequence-Specific Resonance Assignments: Connecting Spin Systems.- 4.3. Resolving Resonance Overlap.- 5. Protein Structure Analysis with Sequential Assignment Data.- References.- 5 Solid-State NMR Spectroscopy of Proteins.- 1. Introduction.- 2. Protein Dynamics.- 2.1. Backbone Motions.- 2.2. Sidechain Motions.- 3. Protein Structure.- 3.1. Oriented Samples.- 3.2. Unoriented Samples.- 4. Perspective.- References.- 6 Methods for Suppression of the H2O Signal in Proton FT/NMR Spectroscopy: A Review.- 1. Introduction.- 2. Frequency-Selective Excitation.- 2.1. Continuous-Wave and Rapid-Scan Techniques.- 2.2. Tunable Notch Filter.- 2.3. Frequency-Selective Hard Pulse Sequences.- 2.4. Frequency-Selective Soft Pulse Sequences.- 2.5. Tailored Excitation.- 2.6. Nonlinear Excitation.- 3. Selective Presaturation.- 4. Software-Based Methods.- 5. Relaxation Methods.- 5.1. T1-Based Methods.- 5.2. T2-Based Methods.- 5.3. T1? -Based (Spin-Lock).- 6. Polarization Transfer Methods.- 6.1. Heteronulcear Polarization Transfer.- 6.2. Homonuclear Polarization Transfer.- 7. Multiple-Quantum Filtering.- 8. Experimental Comparisons.- 8.1. Redfield 21412 Soft-Pulse Sequence.- 8.2. 11 Hard-Pulse Sequence.- 8.3. 1331 Hard-Pulse Sequence.- References.- of Previous Volumes.

Additional information

Sku

NLS9781461565512

ISBN 13

9781461565512

ISBN 10

1461565510

Title

Biological Magnetic Resonance by Lawrence J. Berliner

Author

Lawrence J. Berliner

Series

Biological Magnetic Resonance

Condition

New

Binding type

Paperback

Publisher

Springer-Verlag New York Inc.

Year published

2012-12-06

Number of pages

264

Prizes

N/A

Cover note

Book picture is for illustrative purposes only, actual binding, cover or edition may vary.

Note

This is a new book - be the first to read this copy. With untouched pages and a perfect binding, your brand new copy is ready to be opened for the first time

Biological Magnetic Resonance Lawrence J. Berliner

Biological Magnetic Resonance by Lawrence J. Berliner

Summary

Biological Magnetic Resonance Summary

Biological Magnetic Resonance by Lawrence J. Berliner

About Lawrence J. Berliner

Table of Contents

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