Arthur G. Palmer III – författare

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

Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy: Principles and Practice develops the complete repertoire of theoretical principals and experimental practices necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy: Principles and Practice is written as a graduate-level textbook and will be of particular interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or who wish to remain abreast of the latest developments in this increasingly important area.* Special Features: * First book to combine detailed NMR theory discussions with experimental applications to biomolecules.* All the theory required to understand these experiments and others.* Easy to follow progression from a fundamental level to an advanced level.* Theory of NMR and practical applications for biomolecular investigations presented.* Theory applied to very practical situations.* Comprehensive treatment of different "levels" of theory from simple ideas to density matrix analysis and operator practices.* Comprehensive description of multi dimensional NMR experiments as applied to unlabeled, 15N-labeled and doubly (13C/15N) labeled proteins.

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