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.
This volume covers state-of-the-art applications of solid-state and solution nuclear magnetic resonance( NMR) spectroscopy to study protein structure, dynamics and interactions. Chapters detail...
Volume 16 marks the beginning of a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. This volume is being followed by Volume 17 with...
NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Fundamentals of Protein NMR Spectroscopy is a comprehensive textbook that...
An introduction to underlying principles and experimental procedures using the newest strategies and techniques for obtaining extensive NMR assignments in biopolymers based on NMR data and the...
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