
Protein NMR Spectroscopy
Principles and Practice
Description
Key Features
- 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
Readership
Table of Contents
PREFACE
PREFACE TO THE FIRST EDITION
ACKNOWLEDGEMENTS
Chapter 1: CLASSICAL NMR SPECTROSCOPY
Chapter 2: THEORETICAL DESCRIPTION OF NMR SPECTROSCOPY
Chapter 3: EXPERIMENTAL ASPECTS OF NMR SPECTROSCOPY
Chapter 4: MULTIDIMENSIONAL NMR SPECTROSCOPY
Chapter 5: RELAXATION AND DYNAMIC PROCESSES
Chapter 6: EXPERIMENTAL 1H NMR METHODS
Chapter 7: HETERONUCLEAR NMR EXPERIMENTS
Chapter 8: EXPERIMENTAL NMR RELAXATION METHODS
Chapter 9: LARGER PROTEINS AND MOLECULAR INTERACTIONS
Chapter 10: SEQUENTIAL ASSIGNMENT, STRUCTURE DETERMINATION, AND OTHER APPLICATIONS
TABLE OF SYMBOLS
LIST OF FIGURES
LIST OF TABLES
SUGGESTED READING
INDEX
SPIN-1/2 PRODUCT OPERATOR EQUATIONS
TABLE OF CONSTANTS
Product details
- No. of pages: 912
- Language: English
- Copyright: © Academic Press 2006
- Published: November 20, 2006
- Imprint: Academic Press
- Hardcover ISBN: 9780121644918
- eBook ISBN: 9780080471037