Nuclear magnetic resonance. Part A, Spectral techniques and dynamics /

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Bibliographic Details
Imprint:San Diego : Academic Press, ©1989.
Description:1 online resource (xxiv, 530 pages) : illustrations.
Language:English
Series:Methods in enzymology ; v. 176
Methods in enzymology ; v. 176.
Subject:
Format: E-Resource Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/11140592
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Varying Form of Title:Spectral techniques and dynamics
Other authors / contributors:Oppenheimer, Norman J.
James, Thomas L.
ISBN:0121820777
9780121820770
Notes:Includes bibliographical references.
Print version record.
Summary:This volume, as does Volume 177, provides a general background of modern NMR techniques, with a specific focus on NMR techniques that pertain to proteins and enzymology, and a "snapshot" of the current state of the art in NMR experimental techniques. These books enable the reader to understand a given technique, to evaluate its strengths and limitations, to decide which is the best approach, and, finally, to design an experiment using the chosen technique to solve a problem.
Other form:Print version: Nuclear magnetic resonance. Part A, Spectral techniques and dynamics. San Diego : Academic Press, ©1989
Table of Contents:
  • Basic Techniques
  • One-Dimensional Nuclear Overhauser Effects and Peak Intensity Measurements
  • Two-Dimensional Nuclear Magnetic Resonance Spectroscopy of Protein: An Overview
  • Solvent Suppression
  • Sample Preparation
  • Advanced Techniques
  • Heteronuclear Nuclear Magnetic Resonance Experiments for Studies of Protein Conformation
  • Multiple-Quantum Nuclear Magnetic Resonance
  • Detection of Insensitive Nuclei
  • Homonuclear Hartmann-Hahn Experiments
  • Two-Dimensional Nuclear Overhauser Effect: Complete Relaxation Matrix Analysis
  • Selective Relaxation Techniques
  • Rotating Frame Nuclear Overhauser Effect
  • Modern Spectrum Analysis in Nuclear Magnetic Resonance: Alternatives to Fourier Transform
  • Solid State Nuclear Magnetic Resonance Structural Studies of Proteins. Enzyme Dynamics: Rate Constants
  • Nuclear Magnetic Resonance Line-Shape Analysis and Determination of Exchange Rates
  • Applicability of Magnetization Transfer Nuclear Magnetic Resonance to Study Chemical Exchange Reactions
  • Two-Dimensional Nuclear Magnetic Resonance Studies of Enzyme Kinetics and Metabolites in Vivo
  • Isotope Exchange
  • Molecular Motions
  • Interpreting Protein Dynamics with Nuclear Magnetic Resonance Relaxation Measurements
  • Solid-State Deuterium Nuclear Magnetic Resonance Spectroscopy of Proteins
  • Protein Rotational Correlation Times by Carbon-13 Rotating-Frame Spin-Lattice Relaxation in Presence of Off-Resonance Radiofrequency Field
  • Measurement of Translational Motion by Pulse-Gradient Spin-Echo Nuclear Magnetic Resonance
  • Structural Characterization of Protein-Folding Intermediates by Proton Nuclear Magnetic Resonance and Hydrogen Exchange
  • Appendix: Computer Programs Related to Nuclear Magnetic Resonance: Availability, Summaries, and Critiques
  • Author Index
  • Subject Index