Nuclear Magnetic Resonance (NMR) spectroscopy, a physical phenomenon based upon the magnetic properties of certain atomic nuclei, has found a wide range of applications in life sciences over recent decades. The dramatic advances in NMR techniques have led to corresponding advances in the ability of NMR to study structure, dynamics and interactions of biological macromolecules in solution under close to physiological conditions. This volume focuses on the use of NMR to study proteins.

NMR can be used to determine detailed three-dimensional structures of proteins in solution. Furthermore, it provides information about conformational or chemical exchange, internal mobility and dynamics at timescales varying from pcoseconds to seconds. It is the primary technique used to obtain information on intrinsically disordered (unfolded) proteins, since these proteins will not crystallize easily. NMR is also a very powerful method for the study of interactions of protein with other molecules, whether small molecules (including drugs), nuclear acids or other proteins.

This up-to-date volume covers NMR techiniques and their application to proteins, with a focus on practical details. This book will provide a newcomer to NMR with the practical guidance in order to carry out successful experiments with proteins and to analyze the resulting spectra. Those who are familiar with the chemical applications of NMR will also find is useful in understanding the special requirements of protien NMR.Content:
Chapter 1 Sample Preparation, Data Collection and Processing (pages 5–21): Frederick W. Muskett
Chapter 2 Isotope Labelling (pages 23–53): Mitsuhiro Takeda and Masatsune Kainosho
Chapter 3 Resonance Assignments (pages 55–82): Lu?Yun Lian and Igor L. Barsukov
Chapter 4 Measurement of Structural Restraints (pages 83–157): Geerten W. Vuister, Nico Tjandra, Yang Shen, Alex Grishaev and Stephan Grzesiek
Chapter 5 Calculation of Structures from NMR Restraints (pages 159–192): Peter Guntert
Chapter 6 Paramagnetic Tools in Protein NMR (pages 193–219): Peter H. J. Keizers and Marcellus Ubbink
Chapter 7 Structural and Dynamic Information on Ligand Binding (pages 221–267): Gordon Roberts
Chapter 8 Macromolecular Complexes (pages 269–317): Paul C. Driscoll
Chapter 9 Studying Partially Folded and Intrinsically Disordered Proteins Using NMR Residual Dipolar Couplings (pages 319–345): Malene Ringkjobing Jensen, Loic Salmon, Gabrielle Nodet, Phineus Markwick, Pau Bernado and Martin Blackledge