Protein NMR Spectroscopy (3rd Ed.)
Principles and Practice


Language: Anglais

Subject for Protein NMR Spectroscopy

Publication date:
784 p. · 19.1x23.5 cm · Hardback

Protein NMR Spectroscopy: Principles and Practice, Third Edition develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments applicable to proteins and other biological macromolecules in solution.

Important new techniques and applications of NMR spectroscopy have emerged since the second edition of this extremely successful book was published in 2006. This third edition includes new sections describing metalloproteins and the application of paramagnetic effects to protein structural elucidation. In addition, the treatments of residual dipolar coupling, intermolecular protein-ligand interactions, relaxation dispersion techniques and larger proteins and requisite labelling schemes are updated and enhanced.

The book is written at a level appropriate for graduate students and practicing biochemists, chemists, biophysicists and structural biologists who utilize NMR spectroscopy as a research tool or who wish to understand the latest developments in the 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 that provides a reference for validation of experimental methods
  • Features detailed derivations of the density matrix formalism and relaxation theory
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 1H 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
Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at North Carolina State University. He is an expert in protein structural biology, particularly in how bacteria are able to protect themselves. Dr. Cavanagh received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of Structural Biology at the Wadsworth Center (New York State Department of Health), Associate Professor of Biomedical Sciences (SUNY) and Professor of Chemistry (Purdue). Since 2000 he has been Professor of Biochemistry in the Department of Molecular & Structural Biochemistry at North Carolina State University. Dr. Cavanagh has served on numerous NIH and NSF grant review panels and is currently a permanent member of the MSFB Study Section at NIH . He has authored over 100 peer-reviewed research publications and has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), the Fullsome Award (1996), the NC State University Alumni Associations Outstanding Research Award (2005) and Entrepreneur of the Year- NC State University (2012). He runs the Jimmy V-NCSU Cancer Therapeutics Training Program, was Assistant Vice Chancellor for Research at NC State from 2012-2014 and is the co-founder and Chief Scientific Officer of Agile Sciences Inc., a Raleigh based biotechnology company focusing on antibiotic resistance.