|
|
|
|
| LEADER |
00000cam a2200000 i 4500 |
| 001 |
SCIDIR_on1082136144 |
| 003 |
OCoLC |
| 005 |
20231120010336.0 |
| 006 |
m o d |
| 007 |
cr cnu|||unuuu |
| 008 |
190114s2019 maua ob 000 0 eng d |
| 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
|d OCLCO
|d OCLCQ
|d OCLCO
|
| 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
|
| 050 |
|
4 |
|a QC762
|b .B565 2019eb
|
| 072 |
|
7 |
|a SCI
|x 038000
|2 bisacsh
|
| 072 |
|
7 |
|a PSD
|2 bicssc
|
| 082 |
0 |
4 |
|a 538/.362
|2 23
|
| 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
|
| 337 |
|
|
|a computer
|b c
|2 rdamedia
|
| 338 |
|
|
|a online resource
|b cr
|2 rdacarrier
|
| 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.
|
| 650 |
|
0 |
|a Nuclear magnetic resonance spectroscopy.
|
| 650 |
|
6 |
|a R�esonance magn�etique nucl�eaire.
|0 (CaQQLa)201-0010725
|
| 650 |
|
6 |
|a Spectroscopie de la r�esonance magn�etique nucl�eaire.
|0 (CaQQLa)201-0072888
|
| 650 |
|
7 |
|a nuclear magnetic resonance.
|2 aat
|0 (CStmoGRI)aat300220368
|
| 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
|
| 700 |
1 |
|
|a Wand, A. Joshua,
|e editor.
|
| 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.
|
| 856 |
4 |
0 |
|u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/615
|z Texto completo
|
