Protein NMR for the Millennium

1. Front Matter

   Pages i-xii

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2. Toward Larger Proteins in Solution and Solid State

   1. Transverse Relaxation Optimized Spectroscopy

      • Konstantin V. Pervushin

      Pages 3-34

   2. Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins

      • Jennifer J. Ottesen, Ulrich K. Blaschke, David Cowburn, Tom W. Muir

      Pages 35-51

   3. Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach

      • David Fushman, David Cowburn

      Pages 53-77

   4. Global Fold Determination of Large Proteins using Site-Directed Spin Labeling

      • John L. Battiste, John D. Gross, Gerhard Wagner

      Pages 79-101

   5. Solid State NMR Studies of Uniformly Isotopically Enriched Proteins

      • Ann McDermott

      Pages 103-120

   6. NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids

      • A. Joshua Wand, Charles R. Babu, Peter F. Flynn, Mark J. Milton

      Pages 121-160

3. Structure Refinement

   1. Angular Restraints from Residual Dipolar Couplings for Structure Refinement

      • Christian Griesinger, Jens Meiler, Wolfgang Peti

      Pages 163-229

   2. Protein Structure Refinement using Residual Dipolar Couplings

      • Angela M. Gronenborn

      Pages 231-253

   3. Hydrogen Bond Scalar Couplings — A New Tool In Biomolecular NMR

      • Stephan Grzesiek, Florence Cordier, Andrew J. Dingley

      Pages 255-283

4. NMR Methods for Screening Bioactive Ligands

   1. NMR Methods for Screening the Binding of Ligands to Proteins — Identification and Characterization of Bioactive Ligands

      • Thomas Peters, Thorsten Biet, Lars Herfurth

      Pages 287-315

5. Back Matter

   Pages 317-341

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Protein NMR for the Millennium is the third volume in a special thematic series devoted to the latest developments in protein NMR under the Biological Magnetic Resonance umbrella. This book is divided into three major sections dealing with significant recent advances in the study of large proteins in solution and solid state, structure refinement, and screening of bioactive ligands.
Key Features:

• TROSY,
• Segmental isotope labeling of proteins,
• Hydrogen bond scalar couplings,
• Structure refinement based on residual dipolar couplings,
• Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.

• magnetic resonance
• positron emission tomography
• protein structure
• proteins
• spectroscopy

`The book is generally easy to read for those with an appreciable knowledge of protein NMR spectroscopy. [...]presents a timely review of many recently developed techniques for the study of large proteins by NMR spectroscopy. We highly recommend it as a reference for anyone with an active interest in this field.'
Journal of the American Chemical Society, 125:51 (2003)

• University of Alabama at Birmingham, Birmingham

  N. Rama Krishna

• University of Denver, Denver

  Lawrence J. Berliner

Dr. N. Rama Krishna is Professor of Biochemistry and Molecular Genetics and the Director of the NMR Core Facility at the University of Alabama at Birmingham. He has previously served as Guest Editor for Volumes 16 (Modern Techniques in Protein NMR, 1998) and Volume 17 (Structure Computation and Dynamics in Protein NMR, 1999). Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He is the Series Editor for Biological Magnetic Resonance, which he launched in 1979.

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