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pt. A ISBN 9780121822392
内容説明
This volume and its companion, Volume 339, supplement Volumes 176, 177, 239, and 261. Chapters are written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.
目次
Contributors to Volume 338.
Preface.
Volume in Series.
Use of Chemical Shifts in Macromolecular Structure Determination, D.S. Wishart and D.A. Case.
Cross-Correlated Relaxation for Measurement of Angles between Tensorial Interactions, H. Schwalbe, T. Carlomagno, M. Hennig, J. Junker, B. Reif, Christian Richter, and C. Griesinger.
Applications of Adiabatic Pulses in Biomolecular Nuclear Magnetic Resonance, E. Kupce.
Scalar Couplings across Hydrogen Bonds, S. Grzesiek, F. Cordier, and A.J. Dingley.
On-Line Cell High-Pressure Nuclear Magnetic Resonance Technique: Application to Protein Studies, K. Akasaka and H. Yamada.
Maximum Entropy Reconstruction: Spectrum Analysis and Deconvolution in Multidimensional Nuclear Magnetic Resonance, J.C. Hoch and A.S. Stern.
Magnetic Relaxation Dispersion Studies of Biomolecular Solutions, B. Halle and V.P. Denisov.
Nuclear Magnetic Resonance-Based Approaches for Lead Generation in Drug Discovery, J.W. Peng, C.A. Lepre, J. Feizo, N. Abdul-Manan, and J.M. Moore.
Screening of Compound Libraries for Protein Binding Using Flow-Injection Nuclear Magnetic Spectroscopists, B.J. Stockman, K.A. Farley, and D.T. Angwin.
The Internet for Nuclear Magnetic Resonance Spectroscopists, S. Farr-Jones and D. Avizonis.
Solid-Phase Synthesis of Selectively Labeled DNA: Applications for Multidimensional Nuclear Magnetic Resonance Spectroscopy, C. Kojima, A.M. Ono, A. Ono, and M. Kainosho.
Uniform 13C/15N-Labeling of DNA by Tandem Repeat Amplification, M.H. Werner, V. Gupta, L.J. Lambert, and T. Nagata.
13C Isotopic Enrichment for Nuclear Magnetic Resonance Studies of Carbohydrates and Glycoconjugates, D. Live, L.A. Silks, J. Schmidt.
Preparation and Use of 2H-Labeled RNA Oligonucleotides in Nuclear Magnetic Resonance Studies, E.P. Nikonowicz.
Investigation of Unusual DNA Motifs, A. Phan, M. Gueron, and J. Leroy.
Resonance Assignment and Structure Determination for RNA, J. Cromsigt, B. van Buuren, J. Schleucher, and S. Wijmenga.
Solution Nuclear Magnetic Resonance Probing of Cation Binding Sites on Nucleic Acids, J. Feigon, S.E. Butcher, L.D. Finger, and N.V. Hud.
Identification and Characterization of Metal Ion Binding Sites in RNA, R.L. Gonzalez and I. Tinoco.
Author Index.
Subject Index.
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pt. B ISBN 9780121822408
内容説明
This volume and its companion, Volume 338, supplement Volumes 176, 177, 239, and 261. Chapters are written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.
目次
Section I: Proteins A. Techniques for proteins
[1]: Physiological Conditions and Practicality for Protein Nuclear Magnetic Resonance Spectroscopy: Experimental Methodologies and Theoretical Background
[2]: Optimization of Protein Solubility and Stability for Protein Nuclear Magnetic Resonance
[3]: Segmental Isotopic Labeling Using Expressed Protein Ligation
[4]: High-Resolution Nuclear Magnetic Resonance of Encapsulated Proteins Dissolved in Low Viscosity Fluids
[5]: Automated Assignment of Ambiguous Nuclear Overhauser Effects with ARIA
[6]: Automatic Determination of Protein Backbone Resonance Assignments from Triple Resonance Nuclear Magnetic Resonance Data
[7]: Nuclear Magnetic Resonance Relaxation in Determination of Residue-Specific 15N Chemical Shift Tensors in Proteins in Solution: Protein Dynamics, Structure, and Applications of Transverse Relaxation Optimized Spectroscopy
[8]: Dipolar Couplings in Macromolecular Structure Determination
[9]: Nuclear Magnetic Resonance Methods for High Molecular Weight Proteins: A Study Involving a Complex of Maltose Binding Protein and ss-Cyclodextrin
[10]: Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules
Section I: Proteins B. Classes of proteins
[11]: Characterizing Protein-Protein Complexes and Oligomers by Nuclear Magnetic Resonance Spectroscopy
[12]: Nuclear Magnetic Resonance Methods for Elucidation of Structure and Dynamics in Disordered States
[13]: Micellar Systems as Solvents in Peptide and Protein Structure Determination
[14]: Nuclear Magnetic Resonance of Membrane-Associated Peptides and Proteins
[15]: Paramagnetic Probes in Metalloproteins
Section II: Macromolecular complexes
[16]: Protein-DNA Interactions
[17]: Nuclear Magnetic Resonance Methods to Study Structure and Dynamics of RNA-Protein Complexes
[18]: Protein-protein interactions probed by nuclear magnetic resonance spectroscopy
[19]: Solid-State Nuclear Magnetic Resonance Techniques for Structural Studies of Amyloid Fibrils
Author Index
Subject Index
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pt. C ISBN 9780121827991
内容説明
The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.
目次
Identification and optimization of protein domains for NMR studies
In-cell NMR spectroscopy
Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining
Cross-correlated relaxation for structure and dynamics
Rapid NMR Data Collection
An Integrated Platform for Automated Analysis of Protein NMR Structures
Rapid Assessment of Protein Structural Stability and Fold Validation via NMR
Determination of Protein Backbone Structures from Residual Dipolar Couplings
Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium
Protein Structure Estimation From Minimal Restraints Using Rosetta
Protein Structure Elucidation From Minimal Data: The CLOUDS and ABACUS Approaches
Elucidation of the Protein Folding Landscape by NMR
Membrane Protein Preparation for TROSY NMR Screening
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP
NMR Experiments on Aligned Samplet of Membrane Proteins
NMR techniques used with very large biological macromolecules in solution
Structure determination of large biological RNAs
Hydrodynamic Models and Computational Methods for NMR relaxation
Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High Molecular Weight Systems
Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for RNA
NMR techniques for identifying the interface of a larger protein-protein complex: cross and transferred cross-saturation experiments
Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy
Structure determination of protein/RNA complexes by NMR
Utilization of NMR-derived fragment leads in drug design
Discovery of Ligands by a Combination of Computational and NMR-based Screening: RNA as an Example Target
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