Protein NMR spectroscopy : principles and practice / John Cavanagh ... [et al.].

Contributor(s):

Cavanagh, John, 1963-

Material type: Text

TextPublication details: Amsterdam ; Boston : Academic Press, Elsevier, c2007.Edition: 2nd edDescription: xxv, 885 p. : ill. ; 24 cm.; Hard BoundISBN:

9780121644918 (alk. paper)

Subject(s):

DDC classification:

572.636 CAV 22

NLM classification:

2007 I-373
QD 96.N8

Online resources:

Contents:

1. Classical NMR Spectroscopy -- 2. Theoretical Description of NMR Spectroscopy -- 3. Experimental Aspects of NMR Spectroscopy -- 4. Multi-Dimensional NMR Spectroscopy -- 5. Relaxation and Dynamic Processes -- 6. Experimental <sup>1</sup>H NMR Methods -- 7. Heteronuclear NMR Experiments -- 8. Experimental NMR Relaxation Methods -- 9. Larger Proteins and Molecular Interactions -- 10. Sequential Assignment, Structure Determination and Other Applications.

Summary: Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field. Provides an understanding of the theoretical principles important for biological NMR spectroscopy Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods

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Holdings
Item type	Current library	Collection	Call number	Status	Date due	Barcode
Books	H.T. Parekh Library	SIAS Collection	572.636 CAV (Browse shelf(Opens below))	Available		K2414

$121.00
TB/236/210720

Includes bibliographical references (p. 839-840) and index.

1. Classical NMR Spectroscopy --
2. Theoretical Description of NMR Spectroscopy --
3. Experimental Aspects of NMR Spectroscopy --
4. Multi-Dimensional NMR Spectroscopy --
5. Relaxation and Dynamic Processes --
6. Experimental <sup>1</sup>H NMR Methods --
7. Heteronuclear NMR Experiments --
8. Experimental NMR Relaxation Methods --
9. Larger Proteins and Molecular Interactions --
10. Sequential Assignment, Structure Determination and Other Applications.

Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field. Provides an understanding of the theoretical principles important for biological NMR spectroscopy Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods

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