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Band 9

Biological Magnetic Resonance

Aus der Reihe Biological Magnetic Resonance

Fr. 143.00

inkl. gesetzl. MwSt., Versandkostenfrei

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

06.12.2012

Herausgeber

Lawrence J. Berliner + weitere

Verlag

Springer Us

Seitenzahl

264

Maße (L/B/H)

22.9/15.2/1.5 cm

Gewicht

388 g

Auflage

Softcover reprint of the original 1st ed. 1990

Sprache

Englisch

ISBN

978-1-4615-6551-2

Beschreibung

Portrait

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.

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

06.12.2012

Herausgeber

Verlag

Springer Us

Seitenzahl

264

Maße (L/B/H)

22.9/15.2/1.5 cm

Gewicht

388 g

Auflage

Softcover reprint of the original 1st ed. 1990

Sprache

Englisch

ISBN

978-1-4615-6551-2

Herstelleradresse

Libri GmbH
Europaallee 1
36244 Bad Hersfeld
DE

Email: GPSR Kontakt

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  • Produktbild: Biological Magnetic Resonance
  • Produktbild: Biological Magnetic Resonance
  • 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.