The Resource NMR of proteins and small biomolecules, volume editor: Guang Zhu ; with contributions by K. Chen ... [et al.]

NMR of proteins and small biomolecules, volume editor: Guang Zhu ; with contributions by K. Chen ... [et al.]

Label
NMR of proteins and small biomolecules
Title
NMR of proteins and small biomolecules
Statement of responsibility
volume editor: Guang Zhu ; with contributions by K. Chen ... [et al.]
Contributor
Subject
Language
eng
Cataloging source
SzZUIDS
Dewey number
543.66
Illustrations
illustrations
Index
index present
Literary form
non fiction
Nature of contents
bibliography
Series statement
Topics in current chemistry,
Series volume
326
Label
NMR of proteins and small biomolecules, volume editor: Guang Zhu ; with contributions by K. Chen ... [et al.]
Publication
Note
ANALYTIC
Bibliography note
Includes bibliographical references and index
http://library.link/vocab/branchCode
  • net
Contents
  • Contents note continued: 2.2.High Power Heteronuclear Decoupling / Xin Zhao -- 2.3.Cross-Polarization / Xin Zhao -- 2.4.Recoupling in MAS Solid-State NMR / Xin Zhao -- 3.Protein Structure Determination by MAS Solid-State NMR / Xin Zhao -- 3.1.Labeling Strategy and Sample Environments / Xin Zhao -- 3.2.Three-Dimensional Structure Determination / Xin Zhao -- 3.3.Ligand Conformation and Binding / Xin Zhao -- 3.4.Structural Changes upon Activation / Xin Zhao -- 3.5.Protein Dynamics / Xin Zhao -- 3.6.Sensitivity Enhancement / Xin Zhao -- 3.7.Structure Determination Based on Chemical Shifts / Xin Zhao -- 4.Perspective / Xin Zhao -- References / Xin Zhao -- 1.Introduction / Ho Sum Tse / Qinglin Wu / Kong Hung Sze / Guang Zhu -- 2.Theories of Dynamic Nuclear Polarization / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu -- 2.1.Continuous-Wave DNP Mechanism / Kong Hung Sze / Qinglin Wu / Guang Zhu / Ho Sum Tse -- 2.2.Pulsed DNP / Kong Hung Sze / Ho Sum Tse / Qinglin Wu / Guang Zhu --
  • Contents note continued: 2.3.Polarizing Agents / Ho Sum Tse / Qinglin Wu / Kong Hung Sze / Guang Zhu -- 3.Instrumentation / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu -- 3.1.Microwave Sources / Kong Hung Sze / Qinglin Wu / Guang Zhu / Ho Sum Tse -- 3.2.Microwave Waveguides / Kong Hung Sze / Ho Sum Tse / Qinglin Wu / Guang Zhu -- 3.3.Probes Used for DNP Experiments / Kong Hung Sze / Qinglin Wu / Guang Zhu / Ho Sum Tse -- 4.Applications / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu -- 4.1.Applications to Small Molecules / Kong Hung Sze / Qinglin Wu / Guang Zhu / Ho Sum Tse -- 4.2.Applications to Biomolecules / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu -- 4.3.Magnetic Resonance Imaging / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu -- 4.4.Multidimensional Time-Domain Experiment for DNP / Ho Sum Tse / Qinglin Wu / Kong Hung Sze / Guang Zhu -- 5.Future Perspectives / Ho Sum Tse / Qinglin Wu / Kong Hung Sze / Guang Zhu --
  • Contents note continued: 3.2.Chemical Shift Perturbation / Hongyan Li / Hongzhe Sun -- 4.NMR in Studies of Paramagnetic Metalloproteins / Hongyan Li / Hongzhe Sun -- 4.1.Paramagnetism-Based Structural Restraints / Hongyan Li / Hongzhe Sun -- 4.2.13C-Detected Protonless NMR / Hongyan Li / Hongzhe Sun -- 5.Perspectives / Hongyan Li / Hongzhe Sun -- References / Hongyan Li / Hongzhe Sun -- 1.NMR Relaxation to Detect Protein Dynamics / Rieko Ishima -- 2.Recent Improvements in the 15N R1, R2, and 15N-{1H} NOE Experiments / Rieko Ishima -- 2.1.Practical Aspects in 15N R2 Experiment / Rieko Ishima -- 2.2.Practical Aspects in 15N R1 Experiment / Rieko Ishima -- 2.3.Practical Aspects in 15N-{1H} NOE Experiment / Rieko Ishima -- 3.Extending Relaxation Measurements Beyond R1, R2, and 15N-(1H) NOE / Rieko Ishima -- 4.Relaxation Dispersion Experiments / Rieko Ishima -- 4.1.Relaxation Dispersion in General / Rieko Ishima -- 4.2.15N CT-CPMG Relaxation Dispersion Experiment / Rieko Ishima --
  • Contents note continued: 3.4.Approaches for Sample Screening / Tabussom Qureshi / Natalie K. Goto -- 4.Methods for Acquisition of Solution NMR Spectra of Membrane Proteins / Natalie K. Goto / Tabussom Qureshi -- 4.1.Isotope Labeling Schemes for Large Protein Complexes / Tabussom Qureshi / Natalie K. Goto -- 4.2.Relaxation Optimization / Natalie K. Goto / Tabussom Qureshi -- 5.Strategies for Membrane Protein Structure Determination by Solution NMR / Tabussom Qureshi / Natalie K. Goto -- 5.1.NOE-Based Methods of Structure Determination / Natalie K. Goto / Tabussom Qureshi -- 5.2.Non-uniform Sampling / Tabussom Qureshi / Natalie K. Goto -- 5.3.Global Folds in the Absence of Long-Range NOEs / Natalie K. Goto / Tabussom Qureshi -- 6.Concluding Remarks / Tabussom Qureshi / Natalie K. Goto -- References / Tabussom Qureshi / Natalie K. Goto -- 1.Introduction / Xin Zhao -- 2.Basic Experimental Techniques Used in Solid-State NMR / Xin Zhao -- 2.1.Magic-Angle Spinning / Xin Zhao --
  • Contents note continued: 4.3.15N Off-Resonance R1u Experiment / Rieko Ishima -- 4.4.Bloch-McConnell Equation and Related Equations / Rieko Ishima -- 4.5.Practical Aspects Parameter Optimization / Rieko Ishima -- References / Rieko Ishima -- 1.Introduction / Natalie K. Goto / Tabussom Qureshi -- 2.Production of Membrane Protein Samples for Solution NMR / Tabussom Qureshi / Natalie K. Goto -- 2.1.Factors Affecting Choice of Expression System / Tabussom Qureshi / Natalie K. Goto -- 2.2.Membrane Protein Expression in E. Coil / Natalie K. Goto / Tabussom Qureshi -- 2.3.Cell-Free Expression Approaches / Natalie K. Goto / Tabussom Qureshi -- 3.Membrane Mimetic Systems for Solution NMR / Tabussom Qureshi / Natalie K. Goto -- 3.1.Micelles / Natalie K. Goto / Tabussom Qureshi -- 3.2.Bicelles / Tabussom Qureshi / Natalie K. Goto -- 3.3.New Developments in Membrane-Mimetic Solvents for Solution NMR / Natalie K. Goto / Tabussom Qureshi --
  • Contents note continued: 4.Interpretation and Implementation / Kang Chen / Nico Tjandra -- 4.1.Approximations / Kang Chen / Nico Tjandra -- 4.2.Common Applications of RDC / Kang Chen / Nico Tjandra -- 4.3.Ensemble Minimization / Kang Chen / Nico Tjandra -- 4.4.Structure of a Ligand in a Bound State / Kang Chen / Nico Tjandra -- 4.5.Structure of Oligomeric State / Kang Chen / Nico Tjandra -- 5.Conclusion / Kang Chen / Nico Tjandra -- References / Kang Chen / Nico Tjandra -- 1.Introduction / Hongyan Li / Hongzhe Sun -- 2.The Contribution of NMR to Structural Metalloproteins / Hongyan Li / Hongzhe Sun -- 2.1.Conventional Method for Structure Determination of Metalloproteins / Hongyan Li / Hongzhe Sun -- 2.2.Utilization of Chemical Shifts to Generate Structures / Hongyan Li / Hongzhe Sun -- 3.Identification of Metal Coordination / Hongyan Li / Hongzhe Sun -- 3.1.Homonuclear and Heteronuclear Metal NMR Spectroscopy / Hongyan Li / Hongzhe Sun --
  • Contents note continued: References / Jaime L. Stark / Robert Powers -- 1.Introduction / Olga Vinogradova / Jun Qin -- 1.1.Chemical Shift Perturbation Mapping / Olga Vinogradova / Jun Qin -- 1.2.Nuclear Overhauser Effect / Olga Vinogradova / Jun Qin -- 1.3.Residual Dipolar Couplings / Olga Vinogradova / Jun Qin -- 1.4.Paramagnetic NMR / Olga Vinogradova / Jun Qin -- 2.Conclusions / Olga Vinogradova / Jun Qin -- References / Olga Vinogradova / Jun Qin -- 1.Introduction / Kang Chen / Nico Tjandra -- 2.Theoretical Expressions / Kang Chen / Nico Tjandra -- 3.Alignment Methods / Kang Chen / Nico Tjandra -- 3.1.Charged Polyacrylamide Gel / Kang Chen / Nico Tjandra -- 3.2.DNA Based Media / Kang Chen / Nico Tjandra -- 3.3.Collagen Gel / Kang Chen / Nico Tjandra -- 3.4.Composite Media / Kang Chen / Nico Tjandra -- 3.5.Conservative Mutation / Kang Chen / Nico Tjandra -- 3.6.RDC/RCSA Accuracy Improvement / Kang Chen / Nico Tjandra --
  • Contents note continued: References / Kong Hung Sze / Qinglin Wu / Ho Sum Tse / Guang Zhu
  • Machine generated contents note: 1.Introduction / Jaime L. Stark / Robert Powers -- 2.NMR Ligand Affinity Screens / Jaime L. Stark / Robert Powers -- 2.1.Ligand-Based NMR Screens / Jaime L. Stark / Robert Powers -- 2.2.Target-Based NMR Screens / Jaime L. Stark / Robert Powers -- 3.Molecular Docking / Jaime L. Stark / Robert Powers -- 3.1.Docking / Jaime L. Stark / Robert Powers -- 3.2.Scoring / Jaime L. Stark / Robert Powers -- 3.3.Protein Flexibility / Jaime L. Stark / Robert Powers -- 3.4.Virtual Screening and Assessment / Jaime L. Stark / Robert Powers -- 4.Combining Molecular Docking with NMR Ligand Affinity Screens / Jaime L. Stark / Robert Powers -- 4.1.Identification of New Therapeutic Targets / Jaime L. Stark / Robert Powers -- 4.2.Rapid Protein[팩gand Structure Determination / Jaime L. Stark / Robert Powers -- 4.3.Lead Identification / Jaime L. Stark / Robert Powers -- 5.Concluding Remarks / Jaime L. Stark / Robert Powers --
Control code
000049126308
Dimensions
24 cm
Extent
xi, 246 p.
Isbn
9783642289163
Other physical details
ill. (chiefly col.)
http://library.link/vocab/recordID
.b26792072
System control number
  • (OCoLC)780477933
  • springer3642289169

Library Locations

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      -38.195656 144.304955
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