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Nuclear Magnetic Resonance, Part B, Structure and Mechanism
 
 

Nuclear Magnetic Resonance, Part B, Structure and Mechanism, 1st Edition

Volume 177: Nuclear Magnetic Resonance Part B

 
Nuclear Magnetic Resonance, Part B, Structure and Mechanism, 1st Edition,Norman Oppenheimer,Thomas James,ISBN9780121820787
 
 
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Methods in Enzymology

Oppenheimer   &   James   

Abelson  &   Simon   

Academic Press

9780121820787

507

229 X 152

Print Book

Hardcover

In Stock

Estimated Delivery Time
USD 54.71
USD 72.95
 
 

Description

This volume, as does Volume 176, 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.

Readership

Biochemists, organic chemists, analytical chemists, biophysicists, physical chemists, and drug company researchers.

Norman Oppenheimer

Affiliations and Expertise

School of Pharmacy, University of California, San Francisco, U.S.A.

Thomas James

Affiliations and Expertise

School of Pharmacy, University of California, San Francisco, U.S.A.

View additional works by Thomas L. James

Nuclear Magnetic Resonance, Part B, Structure and Mechanism, 1st Edition

Enzyme Modifications for Nuclear Magnetic Resonance Studies: J.T. Gerig, Fluorine Nuclear Magnetic Resonance of Fluorinated Ligands. D.M. LeMaster, Deuteration in Protein-Proton Magnetic Resonance. D.C. Muchmore, L.P. McIntosh, C.B. Russell, D.E. Anderson, and F.W. Dahlquist, Expression and Nitrogen-15 Labeling of Proteins for Proton and Nitrogen-15 Nuclear Magnetic Resonance. D.W. Hibler, L. Harpold, M. Dell'Acqua, T. Pourmotabbed, J.A. Gerlt, J.A. Wilde, and P.H. Bolton, Isotopic Labeling with Hydrogen-2 and Carbon-13 to Compare Conformations of Proteins and Mutants Generated by Site-Directed Mutagenesis, I. P.A. Kosen, Spin Labeling of Proteins. Protein Structure: K. W*aduthrich, Determination of Three-Dimensional Protein Structures in Solution by Nuclear Magnetic Resonance: An Overview. V.J. Basus, Proton Nuclear Magnetic Resonance Assignments. M. Billeter, Computer-Assisted Resonance Assignments. I.D. Kuntz, J.F. Thomason, and C.M. Oshiro, Distance Geometry. R.M. Scheek, W.F. van Gunsteren, and R. Kaptein, Molecular Dynamics Simulation Techniques for Determination of Molecular Structures from Nuclear Magnetic Resonance Data. R.B. Altman and O. Jardetzky, Heuristic Refinement Method for Determination of Solution Structure of Proteins from Nuclear Magnetic Resonance Data. I. Bertini, L. Banci, and C. Luchinat, Proton Magnetic Resonance of Paramagnetic Metalloproteins. H.J. Vogel, Phosphorus-31 Nuclear Magnetic Resonance of Phosphoproteins. J.A. Wilde, P.H. Bolton, D.W. Hibler, L. Harpold, T. Pourmotabbed, M. Dell'Acqua, and J.A. Gerlt, Isotopic Labeling with Hydrogen-2 and Carbon-13 to Compare Conformations of Proteins and Mutants Generated by Site-Directed Mutagenesis, II. Enzyme Mechanisms: D.G. Gorenstein and C.B. Post, Phosphorus-31 Nuclear Magnetic Resonance of Enzyme Complexes: Bound Ligand Structure, Dynamics, and Environment. C.R. Sanders II and M.-D. Tsai, Ligand*b1Protein Interactions via Nuclear Magnetic Resonance of Quadrupolar Nuclei. P.R. Rosevear and A.S. Mildvan, Ligand Conformations and Ligand*b1Enzyme Interactions as Studied by Nuclear Overhauser Effect. B.D. Nageswara Rao, Determination of Equilibrium Constants of Enzyme-Bound Reactants and Products by Nuclear Magnetic Resonance. J.M. Risley and R.L. Van Etten, Mechanistic Studies Utilizing Oxygen-18 Analyzed by Carbon-13 and Nitrogen-15 Nuclear Magnetic Resonance Spectroscopy. J.J. Villafranca, Positional Isotope Exchange Using Phosphorus-31 Nuclear Magnetic Resonance. J.J. Villafranca, Paramagnetic Probes of Macromolecules. In Vivo Studies of Enzymatic Material: S.M. Cohen, Enzyme Regulation of Metabolic Flux. J.S. Cohen, R.C. Lyon, and P.F. Daly, Monitoring Intracellular Metabolism by Nuclear Magnetic Resonance. Appendix: Computer Programs Related to Nuclear Magnetic Resonance: Availability, Summaries, and Critiques. Each chapter includes references. Author Index. Subject Index.

Quotes and reviews

@from:Praise for the Volume
@qu:"The wide range of topics embraced in this volume virtually ensures its utility to all those engaged in research on protein structure and function. Some of the Sections, as well as an Appendix provide a useful description of computer programs... their operation and scope... the comprehensive Subject Index a useful adjunct... There is no doubt about the utility of such a volume at the lab bench."
@source:--FEBS LETTERS
@from:Praise for the Series
@qu:"The Methods in Enzymology series represents the gold-standard."
@source:--NEUROSCIENCE
@qu:"Incomparably useful."
@source:--ANALYTICAL BIOCHEMISTRY
@qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
@source:--BIO/TECHNOLOGY
@qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
@source:--CHEMISTRY IN INDUSTRY
@qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
@source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
@qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
@source:--ENZYMOLOGIA
@qu:"A series that has established itself as a definitive reference for biochemists."
@source:--JOURNAL OF CHROMATOGRAPHY
 
 
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