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Protein NMR spectroscopy : practical techniques and applications / ed. by Lu-Yun Lian ...
Mitwirkende(r): Resource type: Ressourcentyp: Buch (Online)Buch (Online)Sprache: Englisch Verlag: Chichester, West Sussex : Wiley, 2011Auflage: Online-AusgBeschreibung: Online-Ressource (1 online resource (xiv, 351 p., [10] p. of col. plates)) : illISBN:- 9781283177788
- 1283177781
- 9781119972013
- 9780470721933
- 547/.7 22
- 547.7
- SCI078000
- QP551
Inhalte:
Zusammenfassung: "This is a must for anyone interested in using solution NMR to study proteins. Summing Up: Highly recommended. Graduate students, researchers/faculty, and professionals/practitioners." (Choice, 1 April 2012).Zusammenfassung: Protein NMR Spectroscopy: Practical Techniques and Applications -- Contents -- List of Contributors -- Introduction -- References -- 1 Sample Preparation, Data Collection and Processing -- 1.1 Introduction -- 1.2 Sample Preparation -- 1.2.1 Initial Considerations -- 1.2.2 Additives -- 1.2.3 Sample Conditions -- 1.2.4 Special Cases -- 1.2.5 NMR Sample Tubes -- 1.2.5.1 3 mm Tubes -- 1.3 Data Collection -- 1.3.1 Locking -- 1.3.2 Tuning -- 1.3.3 Shimming -- 1.3.4 Calibrating Pulses -- 1.3.5 Acquisition Parameters -- 1.3.6 Fast Acquisition Methods -- 1.4 Data Processing -- References -- 2 Isotope Labelling -- 2.1 Introduction -- 2.2 Production Methods for Isotopically Labelled Proteins -- 2.2.1 Recombinant Protein Expression in Living Organisms -- 2.2.1.1 Escherichia coli -- 2.2.1.2 Yeast Cells -- 2.2.1.3 Other Host Cells -- 2.2.2 Cell-Free Synthesis -- Protocol 1: Preparation of the Amino Acid Free S30 Extract -- Protocol 2: Cell-Free Reaction on a Small Scale -- 2.3 Uniform Isotope Labelling of Proteins -- 2.3.1 Uniform 15N Labelling -- 2.3.2 Uniform 13C, 15N Labelling -- 2.3.3 2H Labelling -- 2.4 Selective Isotope Labelling of Proteins -- 2.4.1 Amino Acid Type-Selective Labelling -- 2.4.2 Reverse Labelling -- 2.4.3 Stereo-Selective Labelling -- 2.5 Segmental Labelling -- 2.6 SAIL Methods -- 2.6.1 Concept of SAIL -- 2.6.2 Practical Procedure for the SAIL Method -- Protocol 3: Production of SAIL Proteins by the E. coli Cell-Free Method -- 2.6.3 Residue-Selective SAIL Method -- Protocol 4: Optimisation of the Amount of SAIL Amino Acids for the Production of Calmodulin Selectively Labelled by SAIL Phenylalanine -- 2.7 Concluding Remarks -- Acknowledgements -- References -- 3 Resonance Assignments -- 3.1 Introduction -- 3.2 Resonance Assignment of Unlabelled Proteins -- 3.2.1 Spin System Assignments -- 3.2.2 Sequence-Specific Assignments.PPN: PPN: 807340308Package identifier: Produktsigel: ZDB-26-MYL | ZDB-30-PAD | ZDB-30-PQE
Protein NMR Spectroscopy: Practical Techniques and Applications; Contents; List of Contributors; Introduction; References; 1 Sample Preparation, Data Collection and Processing; 1.1 Introduction; 1.2 Sample Preparation; 1.2.1 Initial Considerations; 1.2.2 Additives; 1.2.3 Sample Conditions; 1.2.4 Special Cases; 1.2.5 NMR Sample Tubes; 1.2.5.1 3 mm Tubes; 1.3 Data Collection; 1.3.1 Locking; 1.3.2 Tuning; 1.3.3 Shimming; 1.3.4 Calibrating Pulses; 1.3.5 Acquisition Parameters; 1.3.6 Fast Acquisition Methods; 1.4 Data Processing; References; 2 Isotope Labelling; 2.1 Introduction
2.2 Production Methods for Isotopically Labelled Proteins2.2.1 Recombinant Protein Expression in Living Organisms; 2.2.1.1 Escherichia coli; 2.2.1.2 Yeast Cells; 2.2.1.3 Other Host Cells; 2.2.2 Cell-Free Synthesis; Protocol 1: Preparation of the Amino Acid Free S30 Extract; Protocol 2: Cell-Free Reaction on a Small Scale; 2.3 Uniform Isotope Labelling of Proteins; 2.3.1 Uniform 15N Labelling; 2.3.2 Uniform 13C, 15N Labelling; 2.3.3 2H Labelling; 2.4 Selective Isotope Labelling of Proteins; 2.4.1 Amino Acid Type-Selective Labelling; 2.4.2 Reverse Labelling; 2.4.3 Stereo-Selective Labelling
2.5 Segmental Labelling2.6 SAIL Methods; 2.6.1 Concept of SAIL; 2.6.2 Practical Procedure for the SAIL Method; Protocol 3: Production of SAIL Proteins by the E. coli Cell-Free Method; 2.6.3 Residue-Selective SAIL Method; Protocol 4: Optimisation of the Amount of SAIL Amino Acids for the Production of Calmodulin Selectively Labelled by SAIL Phenylalanine; 2.7 Concluding Remarks; Acknowledgements; References; 3 Resonance Assignments; 3.1 Introduction; 3.2 Resonance Assignment of Unlabelled Proteins; 3.2.1 Spin System Assignments; 3.2.2 Sequence-Specific Assignments; 3.2.3 Possible Difficulties
3.3 15N-Edited Experiments3.4 Triple Resonance; 3.4.1 3D Triple Resonance; 3.4.1.1 Identification of Spin Systems; 3.4.1.2 Sequential Assignment; 3.4.1.3 Proline Residues; 3.4.2 4D Triple Resonance; 3.4.3 Computer-Assisted Backbone Assignments; 3.4.4 Unstructured Proteins; 3.4.5 Large Proteins; 3.5 Side-Chain Assignments; References; 4 Measurement of Structural Restraints; 4.1 Introduction; 4.2 NOE-Based Distance Restraints; 4.2.1 Physical Background; 4.2.2 NMR Experiments for Measuring the NOE; 4.2.3 Set-up of NOESY Experiments; 4.2.3.1 Estimation of T2s; Recipe 4.1: 1-1 Echo Experiment
Recipe 4.2: Set-up of Optimal Acquisition TimesRecipe 4.3: Set-up of a 3D 15N-Edited NOESY Experiment (Figure 4.2a); Recipe 4.4: Set-up of a 3D 13C-Edited NOESY Experiment; 4.2.4 Deriving Structural Information from NOE Cross-peaks; Recipe 4.5: Extraction of Distances Using Classes; Recipe 4.6: Extraction of Distances Using the Two-Spin Approximation; 4.2.5 Information Content of NOE Restraints; 4.3 Dihedral Restraints Derived from J-Couplings; 4.3.1 Physical Background; 4.3.2 NMR Experiments for Measuring J-Couplings; Recipe 4.7: E.COSY Experiment; Recipe 4.8: Quantitative J-Correlation
4.3.3 Deriving Structural Information from J-Couplings
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