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Nuclear Magnetic Resonance, Part A, Vol 176. Methods in Enzymology

  • ID: 1768884
  • Book
  • November 1989
  • Region: Global
  • 530 Pages
  • Elsevier Science and Technology
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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.

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Basic Techniques: J.A. Ferretti and G.H. Weiss, One-Dimensional Nuclear Overhauser Effects and Peak Intensity Measurements. J.L. Markley, Two-Dimensional Nuclear Magnetic Resonance Spectroscopy of Protein: An Overview. P.J. Hore, Solvent Suppression. N.J. Oppenheimer, Sample Preparation. Advanced Techniques: G. Wagner, Heteronuclear Nuclear Magnetic Resonance Experiments for Studies of Protein Conformation. M. Rance, W.J. Chazin, C. Dalvit, and P.E. Wright, Multiple-Quantum Nuclear Magnetic Resonance. A. Bax, S.W. Sparks, and D.A. Torchia, Detection of Insensitive Nuclei. A. Bax, Homonuclear Hartmann-Hahn Experiments. B.A. Borgias and T.L. James, Two-Dimensional Nuclear Overhauser Effect: Complete Relaxation Matrix Analysis. N. Niccolai and C. Rossi, Selective Relaxation Techniques. L.R. Brown and B.T. Farmer II, Rotating Frame Nuclear Overhauser Effect. J.C. Hoch, Modern Spectrum Analysis in Nuclear Magnetic Resonance: Alternatives to Fourier Transform. S.J. Opella and P.L. Stewart, Solid State Nuclear Magnetic Resonance Structural Studies of Proteins. Enzyme Dynamics: Rate Constants: B.D.N. Rao, Nuclear Magnetic Resonance Line-Shape Analysis and Determination of Exchange Rates. J.J Led, H. Gesmar, and F. Abildgaard, Applicability of Magnetization Transfer Nuclear Magnetic Resonance to Study Chemical Exchange Reactions. B. Berkowitz and R.S. Balaban , Two-Dimensional Nuclear Magnetic Resonance Studies of Enzyme Kinetics and Metabolites in Vivo. P. R*adosch, Isotope Exchange. Molecular Motions: R.E. London, Interpreting Protein Dynamics with Nuclear Magnetic Resonance Relaxation Measurements. M.A. Keniry, Solid-State Deuterium Nuclear Magnetic Resonance Spectroscopy of Proteins. T. Schleich, C.F. Morgan, and G.H. Caines, Protein Rotational Correlation Times by Carbon-13 Rotating-Frame Spin-Lattice Relaxation in Presence of Off-Resonance Radiofrequency Field. R.L. Haner and T. Schleich, Measurement of Translational Motion by Pulse-Gradient Spin-Echo Nuclear Magnetic Resonance. H. Roder, 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.
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Abelson, John N.
Simon, Melvin I.
Oppenheimer, Norman J.
James, Thomas L.

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