http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
XII, 341 p. 127 illus., 1 illus. in color. online resource.
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.
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.
edited by N. Rama Krishna, Lawrence J. Berliner.
Atomic, Molecular, Optical and Plasma Physics