Biological NMR. Part B /
Saved in:
| Imprint: | Cambridge, MA : Academic Press, 2019. |
|---|---|
| Description: | 1 online resource (xvii, 526 pages) : illustrations |
| Language: | English |
| Series: | Methods in enzymology ; volume 615 Methods in enzymology ; v. 615. |
| Subject: | |
| Format: | E-Resource Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/12379302 |
MARC
| LEADER | 00000cam a2200000Ii 4500 | ||
|---|---|---|---|
| 001 | 12379302 | ||
| 005 | 20200828225658.5 | ||
| 006 | m o d | ||
| 007 | cr cnu|||unuuu | ||
| 008 | 190114s2019 maua ob 000 0 eng d | ||
| 015 | |a GBB917868 |2 bnb | ||
| 016 | 7 | |a 019214124 |2 Uk | |
| 019 | |a 1082324362 | ||
| 020 | |a 9780128167632 |q (electronic bk.) | ||
| 020 | |a 0128167637 |q (electronic bk.) | ||
| 020 | |z 9780128167625 | ||
| 020 | |z 0128167629 | ||
| 035 | |a (OCoLC)1082136144 |z (OCoLC)1082324362 | ||
| 035 | 9 | |a (OCLCCM-CC)1082136144 | |
| 037 | |a 9780128167632 |b Ingram Content Group | ||
| 040 | |a N$T |b eng |e rda |e pn |c N$T |d MEU |d OPELS |d YDX |d EBLCP |d N$T |d UKMGB |d OCLCF |d BRX |d AU@ |d OCLCQ | ||
| 049 | |a MAIN | ||
| 050 | 4 | |a QC762 |b .B565 2019eb | |
| 072 | 7 | |a SCI |x 038000 |2 bisacsh | |
| 072 | 7 | |a PSD |2 bicssc | |
| 245 | 0 | 0 | |a Biological NMR. |n Part B / |c [edited by] A. Joshua Wand. |
| 264 | 1 | |a Cambridge, MA : |b Academic Press, |c 2019. | |
| 300 | |a 1 online resource (xvii, 526 pages) : |b illustrations | ||
| 336 | |a text |b txt |2 rdacontent |0 http://id.loc.gov/vocabulary/contentTypes/txt | ||
| 337 | |a computer |b c |2 rdamedia |0 http://id.loc.gov/vocabulary/mediaTypes/c | ||
| 338 | |a online resource |b cr |2 rdacarrier |0 http://id.loc.gov/vocabulary/carriers/cr | ||
| 490 | 1 | |a Methods in enzymology ; |v volume 615 | |
| 546 | |a Text in English. | ||
| 504 | |a Includes bibliographical references. | ||
| 505 | 0 | |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 | |
| 505 | 8 | |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 | |
| 505 | 8 | |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 | |
| 505 | 8 | |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 | |
| 505 | 8 | |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 | |
| 650 | 0 | |a Nuclear magnetic resonance. |0 http://id.loc.gov/authorities/subjects/sh85093005 | |
| 650 | 0 | |a Nuclear magnetic resonance spectroscopy. |0 http://id.loc.gov/authorities/subjects/sh85093008 | |
| 650 | 7 | |a SCIENCE |x Physics |x Magnetism. |2 bisacsh | |
| 650 | 7 | |a Nuclear magnetic resonance. |2 fast |0 (OCoLC)fst01040325 | |
| 650 | 7 | |a Nuclear magnetic resonance spectroscopy. |2 fast |0 (OCoLC)fst01040333 | |
| 655 | 4 | |a Electronic books. | |
| 700 | 1 | |a Wand, A. Joshua, |e editor. |1 http://viaf.org/viaf/44155707008822411556 | |
| 776 | 0 | 8 | |i Print version: |t Biological NMR. Part B. |d Cambridge, MA : Academic Press, 2019 |z 0128167629 |z 9780128167625 |w (OCoLC)1040989076 |
| 830 | 0 | |a Methods in enzymology ; |v v. 615. |0 http://id.loc.gov/authorities/names/n42016419 | |
| 903 | |a HeVa | ||
| 929 | |a oclccm | ||
| 999 | f | f | |i 76d03c7c-4524-514b-bf26-6aa7cc210f2d |s 4d92f7fa-1021-5a6f-abfe-0ba94697d9a8 |
| 928 | |t Library of Congress classification |a QC762 .B565 2019eb |l Online |c UC-FullText |u https://www.sciencedirect.com/science/bookseries/00766879/615 |z Elsevier |g ebooks |i 11979382 | ||