Nuclear Magnetic Resonance, Part C: Volume 239

Nuclear Magnetic Resonance, Part C: Volume 239

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Nuclear Magnetic Resonance Spectroscopy is the only "tool" available for the determination of high-resolution biological molecule structure in solution. This volume includes methods for expeditiously analyzing the vast amount of data produced by the new 3D and 4D NMR techniques and for generating structures from the data and for assessing the quality of those structures. Application to various classes of important proteins and protein-ligand complexes illustrate uses of the methodology presented. Examination of techniques to explore the dynamic nature of proteins complete the volume.
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Product details

  • Hardback | 813 pages
  • 154 x 232 x 42mm | 1,238.32g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 0121821404
  • 9780121821401

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Praise for the Volume
"Applications of high-resolution NMR techniques to biological systems have advances significantly since the publication of the two previous volumes in 1989. This book succeeds in covering these developments in an authoritative andcomprehensive manner... The serious investigator will be rewarded with an in-depth understanding of much that is important in modern protein NMR spectroscopy."
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
"Incomparably useful."
"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."
"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."
"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."
"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."
"A series that has established itself as a definitive reference for biochemists."
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Table of contents

Techniques: A. Experimentation:
A.S. Edison, F. Abildgaard, W.M. Westler, E.S. Mooberry, and J.L. Markley, Practical Introduction to Theory and Implementation of Multinuclear, Multidimensional Nuclear Magnetic Resonance Experiments.
G.W. Vuister, S. Grzesiek, F. Delaglio, A.C. Wang, R. Tschudin, G. Zhu, and A. Bax, Measurement of Homo- and Heteronuclear J Couplings from Quantitative J Correlation.
S.I. Macura, W.M. Westler, and J.L. Markley, Two-Dimensional Exchange Spectroscopy of Proteins.
J. Keeler, R.T. Clowes, A.L. Davis, and E.D. Laue, Pulsed-Field Gradients: Theory and Practice.
L. Emsley, Selective Pulses and Their Applications to Assignment and Structure Determination in Nuclear Magnetic Resonance.
E.S. Mooberry, F. Abildgaard, and J.L. Markley, Modifications of Older Model Nuclear Magnetic Resonance Console for Collection of Multinuclear, Multidimensional Spectral Data.
B. Data Processing:
P.N. Borer and G.C. Levy, Using Maximum Likelihood Spectral Deconvolution in Multidimensional Nuclear Magnetic Resonance.
M. Kjaer, K.V. Andersen, and F.M. Poulsen, Automated and Semiautomated Analysis of Homo- and Heteronuclear Multidimensional Nuclear Magnetic Resonance Spectra of Proteins: The Program Pronto.
H. Oschkinat and D. Croft, Automated Assignment of Multidimensional Nuclear Magnetic Resonance Spectra.
J.J. Led and H. Gesmar, Quantitative Information from Complicated Nuclear Magnetic Resonance Spectra of Biological Macromolecules.
Protein Structure: A. General:
G.M. Clore and A.M. Gronenborn, Multidimensional Heteronuclear Nuclear Magnetic Resonance of Proteins.
D.S. Wishart and B.D. Sykes, Chemical Shifts as a Tool for Structure Determination.
D.A. Case, H.J. Dyson, and P.E. Wright, Use of Chemical Shifts and Coupling Constants in Nuclear Magnetic Resonance Structural Studies on Peptides and Proteins.
T.L. James, Assessment of Quality of Derived Macromolecular Structures.
B. Classes of Proteins:
Y. Arata, K. Kato, H. Takahashi, and I. Shimada, Nuclear Magnetic Resonance Study of Antibodies: A Multinuclear Approach.
P.N. Barlow and I.D. Campbell, Strategy for Studying Modular Proteins: Application to Complement Modules.
L. Bancil, I. Bertini, and C. Luchinat, Two-Dimensional Nuclear Magnetic Resonance Spectra of Paramagnetic Systems.
G.D. Henry and B.D. Sykes, Methods to Study Membrane Protein Structure in Solution.
S.J. Opella, Y. Kim, and P. McDonnell, Experimental Nuclear Magnetic Resonance Studies of Membrane Proteins.
Dynamics and Disorder:
J.W. Peng and G. Wagner, Investigation of Protein Motions via Relaxation Measurements.
A.N. Lane and J.-F. Lefovre, Nuclear Magnetic Resonance Measurements of Slow Conformational Dynamics in Macromolecules.
W.F. van Gunsteren, R.M. Brunne, P. Gros, R.C. van Schaik, C.A. Schiffer, and A.E. Torda, Accounting for Molecular Mobility in Structure Determination Based on Nuclear Magnetic Resonance Spectroscopic and X-Ray Diffraction Data.
Protein-Ligand Interactions:
L.Y. Lian, I.L. Barsukov, M.J. Sutcliffe, K.H. Sze, and G.C.K. Roberts, Protein-Ligand Interactions: Exchange Processes and Determination of Ligand Conformation and Protein-Ligand Contacts.
A.J. Wand and J.H. Short, Nuclear Magnetic Resonance Studies of Protein-Peptide Complexes.
A.M. Petros and S.W. Fesik, Nuclear Magnetic Resonance Methods for Studying Protein-Ligand Complexes.
D.E. Wemmer and P.G. Williams, Use of Nuclear Magnetic Resonance in Probing Ligand-Macromolecule Interactions.
Author Index.
Subject Index.
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