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1.

図書

図書
edited by Lawrence J. Berliner, Gareth R. Eaton and Sandra S. Eaton
出版情報: New York : Kluwer Academic/Plenum Publishers, c2000  xviii, 614 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 19
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2.

図書

図書
edited by Oleg Y. Grinberg and Lawrence J. Berliner
出版情報: New York : Kluwer Academic/Plenum Publishers, c2004  xxi, 569 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 22
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3.

図書

図書
edited by Sandra R. Eaton, Gareth R. Eaton, and Lawrence J. Berliner
出版情報: New York : Kluwer Academic/Plenum Publishers, 2005  xxiv, 522 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 23. Biomedical EPR ; pt. A
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Saturation Recovery
Loop Gap Resonators
EPR Interfaced to Rapid Mixing
Applications of Angle Selected Electrons Nuclear Double Resonance to Characterize Structure Solvent in Small Molecules and Macromolecules
Solution-ENDOR of Some biologically Interesting Radical Ions
Electron-Electron Double Resonance
Digital Detection in EPR
Distance Measurement by Pulse EPR-ESR and Molecular Dynamics
Site-Directed Spin Labeling
Saturation Transfer Studies of Biological Membranes
Saturation Transfer EPR: Rotational Dynamics of Membrane Proteins
Trends in EPR Technology
Prognosis
Index
Saturation Recovery
Loop Gap Resonators
EPR Interfaced to Rapid Mixing
4.

図書

図書
edited by Sandra R. Eaton, Gareth R. Eaton, and Lawrence J. Berliner
出版情報: New York : Kluwer Academic/Plenum Publishers, 2005  xxiii, 470 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 24. Biomedical EPR ; pt. B
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Saturation Recovery
Loop Gap Resonators
EPR Interfaced to Rapid Mixing
Applications of Angle Selected Electrons Nuclear Double Resonance to Characterize Structure Solvent in Small Molecules and Macromolecules
Solution-ENDOR of Some biologically Interesting Radical Ions
Electron-Electron Double Resonance
Digital Detection in EPR
Distance Measurement by Pulse EPR-ESR and Molecular Dynamics
Site-Directed Spin Labeling
Saturation Transfer Studies of Biological Membranes
Saturation Transfer EPR: Rotational Dynamics of Membrane Proteins
Trends in EPR Technology
Prognosis
Index
Saturation Recovery
Loop Gap Resonators
EPR Interfaced to Rapid Mixing
5.

図書

図書
edited by Lawrence J. Berliner and Christopher J. Bender
出版情報: New York : Kluwer Academic/Plenum publishers, c2004  vi, 437 p. ; 26 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 21
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6.

図書

図書
edited by N. Rama Krishna and Lawrence J. Berliner
出版情報: New York : Kluwer Academic/Plenum Publishers, c1999  xxi, 554 p ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 17
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Computational Methods / Section I.:
Aspects of Modeling Biomolecular Structure on the Basis of Spectroscopic or Diffraction Data / Wilfred F. van Gunsteren ; Alexandre M. J. J. Bonvin ; Xavier Daura ; Lorna J. SmithChapter 1:
Introduction / 1.:
The Molecular Modeling Approach / 2.:
Generating Ensembles Consistent with Experimental Data / 3.:
Six Aspects of Structure Determination Based on Experimental Data / 4.:
Choice of Degrees of Freedom r for Generating an Ensemble and for Calculating q(r) / 4.1.:
Choice of Physical Force Field V[superscript phys](r) / 4.2.:
Choice of (Empirical) Function q(r) for Calculating the Quantity q Using r / 4.3.:
Choice of Penalty Function V[superscript qr] ([q(r)][subscript r]; q[superscript obs]) to Restrain [q(r)][subscript r] to q[superscript obs] / 4.4.:
Quality of the Experimental Data q[superscript obs] to Guide the Restraining / 4.5.:
Choice of Method and Extent of Boltzmann Sampling of the Configurational Space / 4.6.:
Assessing the Quality of the Obtained Ensemble of Structures / 5.:
Pitfalls That Can Be Avoided / 6.:
References
Combined Automated Assignment of NMR Spectra and Calculation of Three-Dimensional Protein Structures / Yuan Xu ; Catherine H. Schein ; Werner BraunChapter 2:
Computational Methods for Sequence-Specific Resonance Assignments
Graph Theory / 2.1.:
Genetic Algorithms and Mutual Information Method / 2.2.:
Neural Networks / 2.3.:
Matching Rungs on a Ladder: Automated Sequential Assignment Using Isotopically Labeled Proteins / 2.4.:
Combinatorial Optimization and Monte Carlo Simulated Annealing of Score Functions / 2.5.:
Real-Space Assignment / 2.6.:
Automated Stereospecific Assignments
Concepts / 3.1.:
Tests, Applications, and Assessment / 3.2.:
Combined Automated NOESY Spectra Assignment and 3D Structure Calculation
Molecular Dynamics Calculations with Ambiguous Restraints
Self-Correcting Distance Geometry Method
Future Improvements and Outlook
NMR Pulse Sequences and Computational Approaches for Automated Analysis of Sequence-Specific Backbone Resonance Assignments of Proteins / Gaetano T. Montelione ; Carlos B. Rios ; G. V. T. Swapna ; Diane E. ZimmermanChapter 3:
Systems for Automated Analysis of Resonance Assignments from Triple-Resonance NMR Spectra
Autoassign
The Algorithm
The Philosophy of AUTOASSIGN
Generic Spin System Objects / 3.3.:
Constraint Propagation / 3.4.:
Representative Results / 3.5.:
Practical Considerations in Data Collection and Processing
General Considerations
Peak Picking of NMR Spectra
Validation of Input Files
Experiments for Automated Analysis of Backbone Resonance Assignments
HSQC / 5.1.:
HNCO / 5.2.:
HN(CA)CO / 5.3.:
HNCA / 5.4.:
HACA(CO)NH / 5.5.:
HACANH / 5.6.:
C-C and C-H Phase Information in HACA(CO)NH and HACANH Experiments / 5.7.:
CBCA(CO)NH / 5.8.:
CBCANH / 5.9.:
C-C and C-H Phase Information in CBCA(CO)NH and CBCANH Experiments / 5.10.:
Future Developments
Calculation of Symmetric Oligomer Structures from NMR Data / Sean I. O'Donoghue ; Michael NilgesChapter 4:
Summary
Symmetry in Macromolecular Aggregates
The Problem: Symmetry Degeneracy in NMR Spectra
Reducing Symmetry Degeneracy with Asymmetric Labeling
The Symmetry-ADR Calculation Method
Symmetry Restraint Terms
Ambiguous Distance Restraints (ADRs)
Annealing Protocols
Iterative Structure Calculation and Explicit Assignment of ADRs
Other Restraint Terms
Experiences with the Symmetry-ADR Method
Initial Test Calculations
ssDBP Dimer
Leucine Zipper Homodimers
p53 Tetramerization Domain
Symmetric Oligomers Solved by NMR
Discussion
Problems of the Symmetry-ADR Method / 6.1.:
Should Symmetry Restraint Terms Be Used? / 6.2.:
Alternatives to the Symmetry-ADR Method / 6.3.:
Symbols
Hybrid-Hybrid Matrix Method for 3D NOESY-NOESY Data Refinements / Elliott K. Gozansky ; Varatharasa Thiviyanathan ; Nishantha Illangasekare ; Bruce A. Luxon ; David G. GorensteinChapter 5:
Simulation Studies Describing 3D NOESY-NOESY Cross Peaks, Approximate versus Exact Methods
Hybrid-Hybrid Relaxation Matrix Method for 3D NOESY-NOESY Data Analysis
Theory and Methods: Deconvolution of 2D NOESY Volumes from 3D NOESY-NOESY Volumes
Three-Dimensional Simulation Test and Effect of Added Noise
Hybrid-Hybrid Relaxation Matrix Structural Refinement of Duplex DNA from Simulated 3D NOESY-NOESY Data
Hybrid-Hybrid Matrix: Experimental Refinement Test on a DNA Three-Way Junction
Conclusions
Conformational Ensemble Calculations: Analysis of Protein and Nucleic Acid NMR Data / Anwer Mujeeb ; Nikolai B. Ulyanov ; Todd M. Billeci ; Shauna Farr-Jones ; Thomas L. JamesChapter 6:
Determination of Structural Restraints
Interproton Distance Restraints
Coupling Constants and Torsion-Angle Restraints
Other Types of Restraints
Indices of Agreement
Assessment of Conformational Flexibility
Ensemble Calculations
Overview
Relaxation-Rate-Based Probability Calculations
Experimental Examples
[omega]-Conotoxin MVIIC
Nucleic Acid Example
Complete Relaxation and Conformational Exchange Matrix (CORCEMA) Analysis of NOESY Spectra of Reversibly Forming Ligand-Receptor Complexes / Chapter 7:
Application to Transferred NOESY / N. Rama Krishna ; Hunter N. B. Moseley
Molecular Complexes and Conformational Exchange / 1.1.:
Reversible Binding and Transferred NOESY / 1.2.:
CORCEMA Theory
Basic Formulation
Two-State Model of Ligand-Receptor Interactions
Treatment for More than Two States
Intermolecular Transferred NOESY
Treatment of Nonspecific Binding
Methods
The CORCEMA Program
Calculation of Concentrations
Methods for Suppressing or Identifying Protein-Mediated Effects
Methods for Observing Intermolecular Transferred NOESY Contacts
Structure Refinement Calculations
Characterization of Some Critical Factors Using Simulated Transferred NOESY Data
Finite Receptor Off-Rates
Effect of Ligand-Receptor Ratio on the Ligand Transferred NOESY
Role of Ligand-Protein Intermolecular Dipolar Relaxation
Ligand-Protein Intermolecular NOESY Intensity as a Function of Off-Rate
Effect of Motions in the Protein-Ligand Complex on the Transferred NOESY
Thrombin-Bound Structures of Human Fibrinopeptide Analogs
Studies on Blood Group A Trisaccharide Bound to Dolichos biflorus Lectin
Transferred NOESY Studies on the Forssman Pentasaccharide Complexed to Dolichos biflorus
Interaction of Sialy1 Lewis[superscript x] Tetrasaccharide with E-selectin
Reversible Binding of Corepressor Tryptophan with Repressor-Operator Complex
Final Comments
Structure and Dynamics / Section II.:
Protein Structure and Dynamics from Field-Induced Residual Dipolar Couplings / James H. Prestegard ; Joel R. Tolman ; Hashim M. Al-Hashimi ; Michael AndrecChapter 8:
Theory
Anisotropic Spin Interactions in Solution-State NMR
The Dipolar Hamiltonian
Residual Dipolar Couplings under Magnetic Field Alignment
Early History of Observation
Application to Protein Systems
Measurement of Residual Dipolar Couplings
Frequency-Domain Experiments
Intensity-Based Experiments
Other Contributions to Multiplet Splittings
Effects of Transverse Relaxation
Dynamic Frequency Shifts
Structure Determination Protocols / 7.:
The Effects of Molecular Motion and Their Separation / 8.:
The Cone-and-Arc Model / 8.1.:
Order Matrix Analysis: A Test for Rigid Model Validity / 8.2.:
Recent Developments in Studying the Dynamics of Protein Structures from [superscript 15]N and [superscript 13]C Relaxation Time Measurements / Jan Engelke ; Heinz RuterjansChapter 9:
General Features of Dynamics
Microdynamic Motional Parameters
Theory of Relaxation in Proteins
Experiments for the Determination of Relaxation Rates
Backbone Dynamics Derived from [superscript 15]N Relaxation Rates
Experimental Details
Processing of Spectra and Determination of Relaxation Rates
Calculation of Microdynamical Parameters
Interpretation of Microdynamical Parameters
Backbone Dynamics Derived from [superscript 13]C[superscript alpha] Relaxation Rates
Analysis of the Multispin Relaxation of [superscript 13]C[superscript alpha]
Experiments to Determine the [superscript 13]C[superscript alpha] Relaxation Rates
Microdynamical Parameters Derived from [superscript 13]C[superscript alpha] Relaxation Rates
Side-Chain Dynamics Derived from [superscript 13]C[superscript beta] Relaxation Rates
Dynamical Parameters Derived from T[subscript 1] Relaxation Times and Steady-State NOE
SIIS Cross Relaxation
Determination of Protein Dynamics in the Microsecond Time Window
Determination of Protein Dynamics in the Millisecond Time Window
Concluding Remarks
Multinuclear Relaxation Dispersion Studies of Protein Hydration / Bertil Halle ; Vladimir P. Denisov ; Kandadai VenuChapter 10:
Methodology of Water NMRD
Conventional Field Variation
Fast Field Cycling
NMR Properties of the Water Nuclei
Relaxation Mechanisms
Quadrupolar Relaxation
Dipolar Relaxation
Relaxation due to Isotropic Couplings
Molecular Motions
Spatial Resolution
Temporal Resolution
Water Relaxation in Semisolid Proteins
Quantitative Analysis of NMRD Data
Parametrization of the NMRD Profile
Correlation Time
Dispersion Amplitude
High-Frequency Plateau
NMRD Time Scales
Stretched Dispersions
Labile Hydrogens
Outlook
Hydration Studies of Biological Macromolecules by Intermolecular Water-Solute NOEs / Gottfried OttingChapter 11:
Theoretical Background for Intermolecular NOEs
NOE between Two Rigidly Bound Protons
NOE between Solute Proton and Bound but Locally Reorientating Water
NOE with Rapidly Diffusing Water Molecules
Assignments of Water-Solute Cross Peaks
NMR Experiments for the Detection of Intermolecular NOEs with Water
Water Suppression
Selective Water Excitation
Nonselective Experiments
Dipolar Field Effects
Applications
Studies of Protein Hydration
Studies of DNA and RNA Hydration
Summary of the Results
Residence Times
Structural Relevance
Future Perspectives
Conclusion
Contents of Previous Volumes
Index
Computational Methods / Section I.:
Aspects of Modeling Biomolecular Structure on the Basis of Spectroscopic or Diffraction Data / Wilfred F. van Gunsteren ; Alexandre M. J. J. Bonvin ; Xavier Daura ; Lorna J. SmithChapter 1:
Introduction / 1.:
7.

図書

図書
edited by Lawrence J. Berliner
出版情報: New York ; London : Plenum Press, c1998  xvii , 423 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 14
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Analysis of Spin Label Lineshapes with Novel Inhomogenous Broadening from Different Component Widths
Application to Spatially Disconnected Domains in Membranes / M.B. Sankarum ; D. Marsh
Progressive Saturation and Saturation transferred EPR for Measuring Exchange Processes and Proximity Relations in Membranes / D. Marsh, et al.
Comparative Spin Label Spectra at X-band (9.5GHz) and W-band (95GHz) / A.I. Smirnov, et al.
Use of Imidazoline Nitroxides in Studies of Chemical Reactions
ESR Measurements of the Concentration and Reactivity of Protons, Thiols, and Nitric Oxide / V. Khramtsov ; L. Volodarsky
ENDOR of Spin-Labels for Structure Determination: From Small Molecules to Enzyme Reaction Intermediates / M.W. Makinen, et al.
Spin-Labeled Nucleic Acids / R.S. Keyes ; A.M. Bobst
Spin Label Applications to Food Science / M.A. Hemminga ; I.J. van den Dries
EPR Studies of Living Animals and Related Model Systems (in Vivo EPR) / H.M. Swartz ; H. Halpern
Index
Analysis of Spin Label Lineshapes with Novel Inhomogenous Broadening from Different Component Widths
Application to Spatially Disconnected Domains in Membranes / M.B. Sankarum ; D. Marsh
Progressive Saturation and Saturation transferred EPR for Measuring Exchange Processes and Proximity Relations in Membranes / D. Marsh, et al.
8.

図書

図書
edited by Lawrence J. Berliner and Jacques Reuben
出版情報: New York : Plenum Press, c1993  xiv, 400 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 13
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9.

図書

図書
edited by Lawrence J. Berliner and Pierre-Marie Robitaille
出版情報: New York ; London : Kluwer Academic, Plenum Publishers, c1998  xv, 255 p. ; 24 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 15
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Tracer Theory and [superscript 13]C NMR / Maren R. Laughlin ; Joanne K. KelleherChapter 1:
Introduction / 1.:
Overview / 1.1.:
Definitions / 1.2.:
Characteristics of a Perfect Tracer / 2.:
Compartmental Models / 3.:
Objectives and Identifiability / 3.1.:
Parameter Estimation and Goodness of Fit / 3.3.:
Linearity and Tracer Models / 3.4.:
The Basic Tracer Experiment / 4.:
General Considerations / 4.1.:
Single Pool Model / 4.2.:
Multicompartmental Catenary Model / 4.3.:
Saturable Kinetic Processes / 5.:
Condensation Reactions / 6.:
Tissue Heterogeneity / 7.:
Metabolic and Isotopic Steady State, Time-Dependent Experiment / 7.1.:
Tissue Heterogeneity Measured in Pre-Isotopic Steady State / 7.2.:
Fractional Enrichment in the Metabolic and Isotopic Steady-State Experiment / 7.3.:
The [superscript 13]C NMR Experiment / 8.:
Chemical Shift and Spectral Resolution / 8.1.:
Metabolic Perturbation / 8.2.:
Detection Limits / 8.3.:
Correction for Natural Abundance Fractional Enrichment / 8.4.:
Subtraction of Natural Abundance Spectra in in Vivo Experiments / 8.5.:
Sites of Label Entry and Sampling, and Substrate Enrichment / 8.6.:
Fractional Enrichment / 8.7.:
Sensitivity and Time / 8.8.:
Use of Reporter Molecules / 8.9.:
Conclusions / 9.:
References
[superscript 13]C Isotopomer Analysis of Glutamate: A NMR Method to Probe Metabolic Pathways Intersecting in the Citric Acid Cycle / A. Dean Sherry ; Craig R. MalloyChapter 2:
The Role of the Citric Acid Cycle in Substrate Oxidation
Anaplerotic Functions of the Citric Acid Cycle
Quantitation of Glutamate Isotopomers by [superscript 13]C NMR
Relation of Glutamate Isotopomers to Multiplets in the [superscript 13]C NMR Spectrum / 2.1.:
Acquisition of the [superscript 13]C NMR Spectrum / 2.2.:
Quantitation of [superscript 13]C Fractional Enrichment by [superscript 1]H NMR / 2.3.:
Influence of Natural Abundance [superscript 13]C on an Isotopomer Analysis / 2.4.:
Mathematical and Computer Models: Applications for Isotopomer Analysis
The Value of Mathematical Models
Historical Background of Current Modeling Techniques
The Evolution of [superscript 13]C Isotopomers in the Citric Acid Cycle
The Steady-State [superscript 13]C Isotopomer Analysis
The Nonsteady-State Analysis
The Direct C4 Analysis: A Readout of Relative Substrate Utilization
Steady-State Analysis under Nosteady-State Conditions
Absolute Metabolic Fluxes from [superscript 13]C Isotopomer Data
Other Considerations / 10.:
Determination of Metabolic Fluxes by Mathematical Analysis of [superscript 13]C-Labeling Kinetics / John C. Chatham ; Edwin M. ChanceChapter 3:
Approach to Analyzing Labeling Kinetics
Formulation of Model
Numerical Methods
Results and Discussion
Metabolic Flux and Subcellular Transport of Metabolites / E. Douglas LewandowskiChapter 4:
The General Utility of Dynamic-Mode [superscript 13]C NMR: Lessons from the Heart
[superscript 13]C NMR and Metabolic Activity
[superscript 13]C-Enrichment Patterns and Oxidative Metabolism
Fractional Enrichment and [superscript 13]C NMR of Metabolic Flux
Models and Parameters of Glutamate Enrichment
Direct Kinetic Analysis of Dynamic [superscript 13]C NMR Spectra
Metabolic Flux and Regulation from Dynamic [superscript 13]C NMR Spectroscopy
Metabolite Compartmentation Effects on [superscript 13]C Kinetics
[superscript 13]C NMR of Subcellular Transport Rates
Summary / 11.:
Assessing Cardiac Metabolic Rates during Pathologic Conditions with Dynamic [superscript 13]C NMR Spectra / Robert G. Weiss ; Gary GerstenblithChapter 5:
Dynamic [superscript 13]C NMR Spectroscopy in Paradigms of Myocardial Dysfunction: "Stunned" and "Hibernating" Myocardium
"Stunned" Myocardium
"Hibernating" Myocardium
Implications for Distinguishing Types of Dysfunctional Myocardium in the Clinical Setting: In Vivo [superscript 13]C NMR
A Strategy for Measuring TCA Cycle Flux with [superscript 13]C NMR
Dynamic [superscript 13]C NMR Spectroscopy of Glycolysis in Ischemic Preconditioning
Metabolic Changes in Ischemic Preconditioned Hearts
Attenuated Ischemic Acidosis in Preconditioned Hearts
Applications of [superscript 13]C Labeling to Studies of Human Brain Metabolism in Vivo / Graeme F. MasonChapter 6:
Measurement of the TCA Cycle Rate in the Brain
A General Description
Theoretical Basis of the Kinetic Modeling: Mass and Isotope Balance
Overview of Interpretation of the Data by Mathematical Modeling
Methods of Detection Currently in Use for Metabolic Studies of Brain in Vivo
Mathematical Modeling: A Detailed Discussion
Description of Metabolic Flow
Equations and Procedures Used to Determine Model Parameters
Measurement of Glutamate Turnover Rate (V[superscript gt])
Determination of V[superscript x]/V[superscript tca] and V[superscript tca] and C4/C3 Labeling Time Courses
Determination of Glutamate/Glutamine Carbon Flow (V[superscript gln]) / 3.5.:
Derivation of Secondary Parameters
Estimation of Carbon Sources for the TCA Cycle
Determination of CMR[subscript gl]
Brain Oxygen Consumption
Quantitative Analyses of Sensitivities
Glucose Turnover Time / 5.1.:
Exchange of Lactate and Pyruvate / 5.2.:
Effects of Metabolic Intermediates and Aspartate / 5.3.:
Rates of Influx and Efflux of Lactate and Pyruvate / 5.4.:
Exchange Between [alpha]-Ketoglutarate and Glutamate / 5.5.:
Pyruvate Carboxylase / 5.6.:
Pentose Phosphate Shunt / 5.7.:
Glucose Label Scrambling / 5.8.:
Glutamate/Glutamine Carbon Flow / 5.9.:
Summary of Sensitivity Analysis / 5.10.:
Metabolic Compartmentation
Neuronal Activity and Compartmentation / 6.1.:
Effects of Glutamate/Glutamine Compartmentation on Measured V[subscript tca] / 6.2.:
Future of [superscript 13]C-Labeling Studies of the Brain in Vivo
In Vivo [superscript 13]C NMR Spectroscopy: A Unique Approach in the Dynamic Analysis of Tricarboxylic Acid Cycle Flux and Substrate Selection / Pierre-Marie Luc RobitailleChapter 7:
The Interaction between Major Biochemical Pathways and Reactions
The Myoglobin System
The Lactate and Alanine Systems
The Creatine Kinase System
The History of Cellular [superscript 13]C NMR
Post-Steady-State Analysis
The Theory of Post-Steady-State Analysis
In Vivo [superscript 13]C NMR Analysis of Substrate Selection
Contents of Previous Volumes
Index
Tracer Theory and [superscript 13]C NMR / Maren R. Laughlin ; Joanne K. KelleherChapter 1:
Introduction / 1.:
Overview / 1.1.:
10.

図書

図書
[edited by] Christopher J. Bender and Lawrence J. Berliner
出版情報: New York : Springer, c2006  xiii, 218 p. ; 25 cm
シリーズ名: Biological magnetic resonance / edited by Lawrence J. Berliner and Jacques Reuben ; v. 25
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Microwave Amplitude Modulation Technique to Measure Spin-Lattice (T1) and Spin-Spin (T2) Relaxation Times
Improvement in the Measurement of Spin-Lattice Relaxation Time in Electron Paramagnetic Resonance
Quantitative Measurement of Magnetic Hyperfine Parameters and the Physical Organic Chemistry of Supramolecular Systems
New Methods of Simulation of Mn(II) EPR Spectra: Single Crystals, Polycrystalline and Amorphous (Biological) Materials
Density Matrix Formalism of Angular Momentum in Multi-Quantum Magnetic Resonance
Microwave Amplitude Modulation Technique to Measure Spin-Lattice (T1) and Spin-Spin (T2) Relaxation Times
Improvement in the Measurement of Spin-Lattice Relaxation Time in Electron Paramagnetic Resonance
Quantitative Measurement of Magnetic Hyperfine Parameters and the Physical Organic Chemistry of Supramolecular Systems
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