Ebook: Protein NMR for the Millennium

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.

---

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.

Content:
Front Matter....Pages i-xii
Transverse Relaxation Optimized Spectroscopy....Pages 3-34
Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins....Pages 35-51
Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach....Pages 53-77
Global Fold Determination of Large Proteins using Site-Directed Spin Labeling....Pages 79-101
Solid State NMR Studies of Uniformly Isotopically Enriched Proteins....Pages 103-120
NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids....Pages 121-160
Angular Restraints from Residual Dipolar Couplings for Structure Refinement....Pages 163-229
Protein Structure Refinement using Residual Dipolar Couplings....Pages 231-253
Hydrogen Bond Scalar Couplings — A New Tool In Biomolecular NMR....Pages 255-283
NMR Methods for Screening the Binding of Ligands to Proteins — Identification and Characterization of Bioactive Ligands....Pages 287-315
Back Matter....Pages 317-341

---

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.

Content:
Front Matter....Pages i-xii
Transverse Relaxation Optimized Spectroscopy....Pages 3-34
Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins....Pages 35-51
Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach....Pages 53-77
Global Fold Determination of Large Proteins using Site-Directed Spin Labeling....Pages 79-101
Solid State NMR Studies of Uniformly Isotopically Enriched Proteins....Pages 103-120
NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids....Pages 121-160
Angular Restraints from Residual Dipolar Couplings for Structure Refinement....Pages 163-229
Protein Structure Refinement using Residual Dipolar Couplings....Pages 231-253
Hydrogen Bond Scalar Couplings — A New Tool In Biomolecular NMR....Pages 255-283
NMR Methods for Screening the Binding of Ligands to Proteins — Identification and Characterization of Bioactive Ligands....Pages 287-315
Back Matter....Pages 317-341
....