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190114s2019 maua ob 000 0 eng d |
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|a N$T
|b eng
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|e pn
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|d MEU
|d OPELS
|d YDX
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|d UKMGB
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|d OCLCQ
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|a 019214124
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|a 1082324362
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|a 9780128167632
|q (electronic bk.)
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|a 0128167637
|q (electronic bk.)
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|a 9780128167625
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|a 0128167629
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|a (OCoLC)1082136144
|z (OCoLC)1082324362
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|a QC762
|b .B565 2019eb
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|a SCI
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|a PSD
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|a 538/.362
|2 23
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|a Biological NMR.
|n Part B /
|c [edited by] A. Joshua Wand.
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|a Cambridge, MA :
|b Academic Press,
|c 2019.
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|a 1 online resource (xvii, 526 pages) :
|b illustrations
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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|a online resource
|b cr
|2 rdacarrier
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|a Methods in enzymology ;
|v volume 615
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546 |
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|a Text in English.
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|a Includes bibliographical references.
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|a Front Cover; Biological NMR Part B; Copyright; Contents; Contributors; Preface; Chapter One: Companion Simulations and Modeling to NMR-Based Dynamical Studies of Proteins; 1. Introduction; 2. The Generalized NMR Order Parameter; 2.1. Definition; 2.2. Simulation of Order Parameters; 2.3. Interpretation of Experimental and Simulated Order Parameters: The Role of Simple Models; 2.4. Molecular Dynamics Simulation of Methyl Order Parameters; 2.5. Simulation of Aromatic Group Order Parameters; 3. Conformational Entropy and Protein Dynamics; 3.1. Definition and Properties of Entropy
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|a 3.2. Extraction of Conformational Entropy of Proteins4. J-couplings; 5. Residual Dipolar Couplings; 6. Protein Compressibility; 7. Molecular Tumbling; 8. Water Dynamics; Acknowledgment; References; Chapter Two: Reverse Micelle Encapsulation of Proteins for NMR Spectroscopy; 1. Introduction; 2. Sample Composition Considerations; 2.1. Aqueous Phase: Protein and Buffer; 2.2. Surfactants; 2.3. Bulk Alkane; 3. Spectroscopic Considerations; 4. Method for Screening RM Conditions; 4.1. Preparing 10MAG/LDAO Samples; 4.1.1. Adjusting the pH of LDAO; 4.1.2. Completing 10MAG/LDAO Samples
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|a 4.2. Preparing CTAB/Hexanol Samples4.3. Preparing AOT Samples; 5. Method for Preparation of RM Solutions in Propane or Ethane; 5.1. Safety Considerations; 5.2. Preparing Sample Components; 5.3. Procedure for Elevated-Pressure RM Encapsulation; 6. Benchmarking Encapsulation; 7. Conclusions and Outlook; Acknowledgments; References; Chapter Three: Characterizing Protein Hydration Dynamics Using Solution NMR Spectroscopy; 1. Introduction; 2. Theoretical and Practical Considerations; 2.1. Foundation Theory; 2.2. Overcoming Artifacts and Limitations
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|a 3. Preparation of Protein Encapsulated RM Samples3.1. Protein Labeling and Purification; 3.2. RM Encapsulation and Considerations; 4. NMR Spectroscopy and Experimental Setup; 4.1. NOESY and ROESY Experiments; 4.2. Two-Dimensional vs Three-Dimensional Experiments; 4.3. Nonuniform Sampling; 4.4. Identification of Hydrogen Exchange; 4.5. Quantification of Hydrogen Exchange-Relayed Magnetization; 5. Data Collection and Analysis; 5.1. Data Collection; 5.2. General Fitting Strategy; 5.3. Simplified Analysis in the Absence of Hydrogen Exchange; 6. Conclusions; Acknowledgments; References
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|a Chapter Four: Understanding Protein Function Through an Ensemble Description: Characterization of Functional States by F NMR1. 19F-Reporters That Can Be Biosynthetically Incorporated Into Proteins; 2. Approaches to Chemical Tagging of Proteins by 19F Reporters; 3. Improving Delineation of States by 19F NMR; 4. Distinguishing States by Topology Measurements That Focus on Solvent Exposure and Hydrophobicity; 5. Relaxation Experiments and Simple Approaches to Delineating States in Fast and Slow Exchange; 6. Extending Resolution of States by 19F NMR; 6.1. Pseudocontact Shift Reagents
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|a Nuclear magnetic resonance.
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|a Nuclear magnetic resonance spectroscopy.
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|a SCIENCE
|x Physics
|x Magnetism.
|2 bisacsh
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|a Nuclear magnetic resonance.
|2 fast
|0 (OCoLC)fst01040325
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|a Nuclear magnetic resonance spectroscopy.
|2 fast
|0 (OCoLC)fst01040333
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|a Electronic books.
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1 |
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|a Wand, A. Joshua,
|e editor.
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776 |
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|i Print version:
|t Biological NMR. Part B.
|d Cambridge, MA : Academic Press, 2019
|z 0128167629
|z 9780128167625
|w (OCoLC)1040989076
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830 |
|
0 |
|a Methods in enzymology ;
|v v. 615.
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856 |
4 |
0 |
|3 ScienceDirect
|u https://www.sciencedirect.com/science/bookseries/00766879/615
|z Full Text via HEAL-Link
|