Protein NMR Spectroscopy

Principles and Practice

Nonfiction, Science & Nature, Science, Physics, Spectrum Analysis, Biological Sciences, Cytology
Cover of the book Protein NMR Spectroscopy by Wayne J. Fairbrother, Nicholas J. Skelton, Mark Rance, Arthur G. Palmer, III, John Cavanagh, Elsevier Science
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Author: Wayne J. Fairbrother, Nicholas J. Skelton, Mark Rance, Arthur G. Palmer, III, John Cavanagh ISBN: 9780080471037
Publisher: Elsevier Science Publication: July 21, 2010
Imprint: Academic Press Language: English
Author: Wayne J. Fairbrother, Nicholas J. Skelton, Mark Rance, Arthur G. Palmer, III, John Cavanagh
ISBN: 9780080471037
Publisher: Elsevier Science
Publication: July 21, 2010
Imprint: Academic Press
Language: English

Protein NMR Spectroscopy, Second Edition 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, the book 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. This updated version 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.

The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or 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
View on Amazon View on AbeBooks View on Kobo View on B.Depository View on eBay View on Walmart

Protein NMR Spectroscopy, Second Edition 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, the book 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. This updated version 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.

The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or wish to understand the latest developments in this field.

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