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Recent developments in biomolecular NMR
پدید آورنده
edited by Marius Clore, Jennifer Potts.
موضوع
Nuclear magnetic resonance spectroscopy.,Nuclear Magnetic Resonance, Biomolecular.,Structure-activity relationships (Biochemistry)
رده
کتابخانه
کتابخانه مطالعات اسلامی به زبان های اروپایی
محل استقرار
استان:
قم
ـ شهر:
قم
تماس با کتابخانه :
32910706
-
025
1849731209
9781849731201
b587553
Recent developments in biomolecular NMR
[Book]
edited by Marius Clore, Jennifer Potts.
Cambridge, UK
RSC Publishing
©2012.
xv, 347 pages : illustrations ; 24 cm.
RSC biomolecular sciences, 25.
P. 216 --; 10.1 A Brief Refresher on NMR-Focussed Ligand Binding 216 --; 10.1.1 Ligand Binding Thermodynamics and Kinetics 216 --; 10.1.2 Ligand Binding and NMR 218 --; 10.2 The Proton Ligands to Inositol Hexakis Phosphate Take Five Instead of Three Log Units to Complete Binding 221 --; 10.3 The Binding of Inositol Hexakis Phosphate to Hemoglobin: Fast-Exchange Kinetics for Nanomolar Affinity 226 --; 10.4 Non-Canonical Line Broadening in Slow Exchange after Equivalence is Reached 235 --; 10.5 Binding of a 10 kDa Ligand to a 70 kDa Protein Does not Result in Significant Line Broadening of the NMR Signals of the 10 kDa Ligand 242 --; 10.5.1 A View From the DnaJ Perspective 242 --; 10.5.2 A View from the DnaK Perspective 247 --; 10.5.3 Relevance of the J-Domain-DnaK Complex 248 --; Acknowledgements 251 --; References 252 --; Chapter 11 Recent Advances in Biomolecular NMR for Drug Discovery / Carine Farenc Farenc, Carine, Gregg Siegal Siegal, Gregg 254 --; 11.1 Introduction 254 --; 11.2 NMR for Ligand Discovery 255 --; 11.2.1 Protein-Observed NMR 255 --; 11.2.2 Ligand-Observed NMR 257 --; 11.3 Hit Prioritisation 261 --; 11.4 Protein-Ligand Structures 262 --; 11.5 In-Cell NMR Spectroscopy 266 --; 11.6 Perspectives 267 --; References 267 --; Chapter 12 NMR of Membrane Proteins / Mark Bostock Bostock, Mark, Daniel Nietlispach Nietlispach, Daniel 271 --; 12.1 Introduction 271 --; 12.2 Protein Expression 273 --; 12.2.1 Escherichia coli 273 --; 12.2.2 Yeast 274 --; 12.2.3 Baculovirus/Insect Expression 275 --; 12.2.4 Mammalian 276 --; 12.2.5 Cell-Free Expression 276 --; 12.2.6 Directed Evolution 278 --; 12.3 Membrane Mimics 278 --; 12.3.1 Detergents 278 --; 12.3.2 Fluorinated Surfactants 283 --; 12.3.3 Amphipols 284 --; 12.3.4 Problems with Micelles 285 --; 12.3.5 Nanolipoprotein Particles 286 --; 12.3.6 NMR Studies using Nanodiscs 287 --; 12.3.7 Bicelles 287 --; 12.4 Isotope-Labelling Strategies 289 --; 12.5 Structure Determination 292 --; 12.5.1 Paramagnetic Effects 293 --; 12.5.2 Residual Dipolar Couplings 295 --; 12.5.3 Chemical Shift Prediction 297 --; 12.6 NMR Method Development 298 --; 12.6.1 ¹³C Direct Detection 298 --; 12.6.2 Alternative Sampling 299 --; 12.7 Functional Information 300 --; 12.7.1 Dynamics 300 --; 12.7.2 Variation of Experimental Conditions 301 --; 12.7.3 Ligand-Binding Studies 301 --; 12.8 Conclusions 303 --; References 304 Chapter 13 Recent Developments in Biomolecular Solid-State NMR / Victoria A. Higman Higman, Victoria A., Anthony Watts Watts, Anthony 318 --; 13.1 Introduction 318 --; 13.2 Samples 319 --; 13.3 Assignment Strategies 322 --; 13.4 Labelling Strategies 322 --; 13.5 Structure Determination 323 --; 13.6 Dynamics 324 --; 13.7 Static Solid-State NMR 325 --; 13.8 Proton Detection 325 --; 13.9 Ultra-Fast Spinning 326 --; 13.10 Dynamic Nuclear Polarisation 326 --; 13.11 Approaches Using Complementary Techniques 328 --; 13.12 Conclusions and Perspectives 328.
Nuclear magnetic resonance spectroscopy.
Nuclear Magnetic Resonance, Biomolecular.
Structure-activity relationships (Biochemistry)
edited by Marius Clore, Jennifer Potts.
Jennifer Potts
Marius Clore
Royal Society of Chemistry (Great Britain)
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