Protein NMR for the Millennium (Biological Magnetic Resonance)

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.

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.

The non-equivalence of certain magnetization transfer pathways in NMR experiments viewed from the stand point of the decay of evolving coherences known as nuclear spin relaxation was recognized at the very onset of the multidimensional multinuclear NMR (Griffey and Redfield, 1987; Gueron et al., 1983; Rance, 1988; Shimizy, 1964). The contributors to this volume deal with significant advances in the study of large proteins in solution and solid state, structure refinement and screening of bioactive ligands