Protein NMR for the Millennium

2002
ISBN: 978-0-306-47448-4
Verlag: Springer US

Buch, Englisch, Band 20, 341 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 765 g

Reihe: Biological Magnetic Resonance

is the third volume in a special thematic series devoted to the latest developments in protein NMR under the 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.

Zielgruppe

Research

Autoren/Hrsg.

Berliner, Lawrence J.

Krishna, N. Rama

Fachgebiete

• Naturwissenschaften Biowissenschaften Proteinforschung
• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
• Naturwissenschaften Chemie Physikalische Chemie
• Naturwissenschaften Physik Thermodynamik Plasmaphysik
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Medizinische Fachgebiete Bildgebende Verfahren, Nuklearmedizin, Strahlentherapie Nuklearmedizin, PET, Radiotherapie
• Naturwissenschaften Biowissenschaften Angewandte Biologie Biophysik
• Naturwissenschaften Physik Quantenphysik Atom- und Molekülphysik
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Medizinische Fachgebiete Bildgebende Verfahren, Nuklearmedizin, Strahlentherapie Radiologie, Bildgebende Verfahren
• Naturwissenschaften Physik Angewandte Physik Biophysik

Inhaltsverzeichnis

Transverse Relaxation Optimized Spectroscopy.- Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins.- Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach.- Global Fold Determination of Large Proteins using Site-Directed Spin Labeling.- Solid State NMR Studies of Uniformly Isotopically Enriched Proteins.- NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids.- Angular Restraints from Residual Dipolar Couplings for Structure Refinement.- Protein Structure Refinement using Residual Dipolar Couplings.- Hydrogen Bond Scalar Couplings — A New Tool In Biomolecular NMR.- NMR Methods for Screening the Binding of Ligands to Proteins — Identification and Characterization of Bioactive Ligands.

Über Autor(innen)

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 (, 1998) and Volume 17 (, 1999). 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 , which he launched in 1979.