Biological Magnetic Resonance

by Lawrence J. Berliner (Editor), Jacques Reuben (Editor)

Overview

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

Product Details

ISBN-13:	9781461565512
Publisher:	Springer US
Publication date:	12/06/2012
Series:	Biological Magnetic Resonance , #9
Edition description:	Softcover reprint of the original 1st ed. 1990
Pages:	264
Product dimensions:	5.98(w) x 9.02(h) x 0.02(d)

About the Author

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.

Table of Contents

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° — t1 — 90° ——m — 90° — 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.

Editorial Reviews

Some of the pioneers in the field explain the use of nuclear magnetic resonance and electron spin resonance spectroscopy to observe and monitor the physiology and pathology of internal organs and tissues. Among the topics are clinical localization techniques, studying brain ischemia, animal studies, and techniques using sodium, fluoride, and hydrogen. Annotation c. Book News, Inc., Portland, OR (booknews.com)

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