N. Rama Krishna / Lawrence J. Berliner (Hgg.)

Protein NMR for the Millennium

Herausgeber: Krishna, N. Rama, Berliner, Lawrence J.

• Gebundenes Buch

Produktbeschreibung

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.

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Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.

Produktdetails

• Biological Magnetic Resonance 20
• Verlag: Springer Netherlands
• 2002
• Seitenzahl: 356
• Erscheinungstermin: 31. Januar 2003
• Englisch
• Abmessung: 241mm x 160mm x 27mm
• Gewicht: 760g
• ISBN-13: 9780306474484
• ISBN-10: 0306474484
• Artikelnr.: 23334315

Autorenporträt

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.

Inhaltsangabe

Section I: Toward Larger Proteins in Solution and Solid State. 1. Transverse Relaxation Optimized Spectroscopy; K.V. Pervushin. 2. Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins; J.J. Ottesen, U.K. Blaschke, D. Cowburn, T.W. Muir. 3. Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach; D. Fushman, D. Cowburn. 4. Global Fold Determination of Large Proteins using Site-Directed Spin Labeling; J.L. Battiste, J.D. Gross, G. Wagner. 5. Solid State NMR Studies of Uniformly Isotopically Enriched Proteins; A. McDermott. 6. NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids; A.J. Wand, C.R. Babu, P.F. Flynn, M.J. Milton. Section II: Structure Refinement. 7. Angular Restraints from Residual Dipolar Couplings for Structure Refinement; C. Griesinger, J. Meiler, W. Peti. 8. Protein Structure Refinement using Residual Dipolar Couplings; A.M. Gronenborn. 9. Hydrogen Bond Scalar Couplings - A New Tool In Biomolecular NMR; S. Grzesiek, F. Cordier, A.J. Dingley. Section III: NMR Methods for Screening Bioactive Ligands. 10. NMR Methods for Screening the Binding of Ligands to Proteins - Identification and Characterization of Bioactive Ligands; T. Peters, T. Biet, L. Herfurth. Index.

Rezensionen

'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)