Protein NMR spectroscopy: practical techniques and applications

ÍNDICE: List of Contributors IntroductionLu-Yun Lian & Gordon Roberts 1 Sample Preparation, Data Collection and ProcessingFrederick W. Muskett 1.1. Introduction 1.2. Sample Preparation 1.3. Data Collection1.4. Data ProcessingReferences 2 Isotope LabellingMitsuhiro Takeda and Masatsune Kainosho 2,1. Introduction 2.2 Production Methods for Isotopically Labelled Proteins2.3 Protocol 1: Preparation of the amino acid free S30 extract2.4 Protocol 2: Cell-Free Reaction on a Small Scale2.5 Uniform Isotope Labelling of Proteins2.6 Selective Isotope Labelling of Proteins2.7 Segmental Labelling2.8 SAIL Methods 2.9 Protocol 3: Production of SAIL Proteins by the E. coli Cell-Free Method2.10 Protocol. 4:Optimisation of the Amount of SAIL Amino Acids for the Production of Calmodulin Selectively Labelled by SAIL Phenylalanine2.11 Concluding RemarksReferences3 Resonance AssignmentsLu-Yun Lian and Igor L. Barsukov 3.1 Introduction 3.2 Resonance Assignment of Unlabelled Proteins3.3 15N-Edited Experiments3.4 Triple Resonance 3.5. Side-Chain AssignmentsReferences 4 Measurement of Structural RestraintsGeerten Vuister, Nico Tjandra, Yang Shen, Alex Grishaev, and StephanGrzesiek 4.1 Introduction4.2 NOE-Based Distance Restraints4.3 Dihedral Restraints Derived from J-Couplings4.4. Hydrogen Bond Restraints4.5 Orientational Restraints4.6 Chemical Shift Structural Restraints4.7 Solution Scattering RestraintsReferences 5 Calculation of Structures from NMR RestraintsPeter Guntert 5.1. Introduction 5.2. Historical Development5.3. Structure Calculation Algorithms5.4. Automated NOE Assignment5.5. Nonclassical Approaches5.6. Fully Automated Structure AnalysisReferences 6 Paramagnetic Tools in Protein NMRPeter H.J. Keizers and Marcellus Ubbink 6.1 Introduction6.2. Types of Restraints6.3. What Metals to Use?6.4. Paramagnetic Probes6.5. Protocol for the Application of Paramagnetic NMR on Diamagnetic Proteins6.6. Examples6.7. Conclusions and PerspectiveReferences 7 Structural and Dynamic Information on Ligand BindingGordon C.K. Roberts 7.1. Introduction7.2. Fundamentals of Exchange Effects on NMR Spectra 7.3. Measurement of Equilibrium and Rate Constants 7.4. Detecting Binding -NMR Screening 7.5. Mechanistic Information7.6. Structural InformationReferences 8 Macromolecular ComplexesPaul C. Driscoll 8.1 Introduction8.2. Spectral Simplification through Differential Isotope Labelling 8.3. Basic NMR Characterisation of Complexes8.4. Protocol of Protein-Protein Titrations8.5. 3D StructureDetermination of Macromolecular Protein-Ligand Complexes8.6. Literature ExamplesReferences 9 Studying Partially Folded and Intrinsically Disordered Proteins using NMR Residual Dipolar CouplingsMalene Ringkjøbing Jensen, Valéry Ozenne, Loic Salmon, Gabrielle Nodet, Phineus Markwick, Pau Bernadó and Martin Blackledge 9.1. Introduction 9.2. Ensemble Descriptions of Unfolded Proteins9.3. Experimental Techniques for the Characterisation of IDPs9.4 NMR Spectroscopy of Intrinsically Disordered Proteins9.5 Residual D

• ISBN: 978-0-470-72193-3
• Editorial: John Wiley & Sons
• Encuadernacion: Cartoné
• Páginas: 384
• Fecha Publicación: 22/07/2011
• Nº Volúmenes: 1
• Idioma: Inglés