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" Nmr as a structural tool for macromolecules. "
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BL
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| Record Number
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727055
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| Doc. No
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b546787
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| Title & Author
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Nmr as a structural tool for macromolecules.
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| Publication Statement
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[Place of publication not identified]: Springer-Verlag New York, 2012
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| ISBN
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1461380294
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: 9781461380290
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| Contents
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Intramolecular Dynamics of Biomolecules. Possibilities and Limitations of NMR (R.R. Ernst et al.). Structural, Dynamic, and Folding Studies of SH2 and SH3 Domains (J.D. FormanKay et al.). NMR Studies of Proteins Involved in Cell Adhesion Processes (G. Wagner et al.). Combining 2H and 13C Selective Enrichment to Probe Protein Dynamics (D.M. LeMaster). Incorporating Motional Properties into the Interpretation of Threedimensional Solution Structures (W.J. Chazin). Phosphotyrosyl Peptideenzyme Complexes: How Much Structure Can We Get from Transferred NOEs? (C.B. Post, M.L. Schneider). Structural Refinement and Dynamics (D. Case et al.). Recent Developments in Protein NMR Spectroscopy (S. Grzesiek et al.). Fieldcycling NMR Applied to Macromolecular Structure and Dynamics (A.G. Redfield). Crosscorrelations: Obstacles or Tools for Structure Determination of Biomolecules (A. Kumar). Toward the Accurate Measurement of Internuclear Distances in Biological Macromolecules by Suppression of Spin Diffusion (S.J.F. Vincent et al.). NMR of Symmetrical Assemblies of Selfrecognizing Oligonucleotides (M. Gueron et al.). Protein-DNA Interaction from NMR and Monte Carlo Docking (R. Kaptein et al.). Dynamic Structure of Nucleic Acid Duplexes (T.L. James et al.). Extension of Techniques to Larger Molecules (G.M. Clore et al.). NMR Structures of Proteins Involved in Signal Transduction (S.W. Fesik et al.). Structures of Multimeric Proteins by NMR (G.M. Clore, A.M. Gronenborn). NMR Structural Studies of Flexible Molecules (P.E. Wright, H.J. Dyson). Iron-Sulfur Proteins: Investigations of Hyperfineshifted Hydrogen, Carbon, and Nitrogen Resonances (B. Xia et al.). On the Use of NMR in ComplexBiological Systems: NMR Studies of Calcium Sensitive Interactionsamong Muscle Proteins (B.D. Sykes et al.). The Structure of Lentiviral Tat Proteins in Solution (R. Roesch et al.). A Structural Biologist's View of Precision and Accuracy of Structural Models ofProteins Based on NMR Data (A.J. Wand). NMR vis a vis Other Structural Methods (B. Brooks et al.). Index.
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| LC Classification
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QP519.9.N83N573 2012
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