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NMR as a Structural Tool for Macromolecules: Current Status and Future Directions

Editat de M.D. Kemple, B.D.N. Rao
en Limba Engleză Paperback – 18 sep 2011
The contemplation of truth and beauty is the proper object for which we were created, which calls forth the most intense desires of the soul, and of which it never tires -Hazlitt In his Nobel lecture Purcell commented that when he saw snow in New England after the discovery of NMR, it appeared like "heaps of protons quietly precessing in earth's magnetic field. " If he were to make the comment in the context of how NMR is being used today, he could have conjured up an image of hydrogen, carbon, and nitrogen nuclei in proteins of an earthbound 8rganism subtly orchestrating a quiet symphony of frequencies, from 150 Hz to 2 kHz, carrying clues to the three-dimensional structure of the macromolecules. The manner in which the basic discoveries of Bloch and Purcell have led to the emergence of NMR, several decades later, as a major technique of biological and medical physics (and chemistry) is a striking example of the power of basic research. It is also a fascinating saga whereby whenever it was felt that the field had reached a plateau, new directions, new technologies, and sometimes serendipity produced new developments that revolutionized the technique and enhanced its capability. As Richard Ernst points out "NMR is intellectually attractive, . . . the practical importance of NMR is enormous, and can justify much of the playful activities of an addicted spectroscopist" (Nobel lecture).
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Specificații

ISBN-13: 9781461380290
ISBN-10: 1461380294
Pagini: 396
Ilustrații: 400 p.
Dimensiuni: 170 x 244 x 21 mm
Greutate: 0.63 kg
Ediția:Softcover reprint of the original 1st ed. 1996
Editura: Springer Us
Colecția Springer
Locul publicării:New York, NY, United States

Public țintă

Research

Cuprins

The Theme of the Symposium.- Keynote Lecture: Intramolecular Dynamics of Biomolecules. Possibilities and Limitations of NMR.- Discussion.- Structural, Dynamic, and Folding Studies of SH2 and SH3 Domains.- Discussion.- NMR Studies of Proteins Involved in Cell Adhesion Processes.- Discussion.- Combining 2H and 13C Selective Enrichment to Probe Protein Dynamics.- Incorporating Motional Properties into the Interpretation of Three-Dimensional Solution Structures.- Discussion.- Phosphotyrosyl Peptide-Enzyme Complexes: How Much Structure Can We Get from Transferred NOE’s?.- Discussion.- Panel Discussion on Structural Refinement and Dynamics.- Recent Developments in Protein NMR Spectroscopy.- Discussion.- Field-Cycling NMR Applied to Macromolecular Structure and Dynamics.- Discussion.- Cross-Correlations: Obstacles or Tools for Structure Determination of Biomolecules.- Discussion.- Towards the Accurate Measurement of Internuclear Distances in Biological Macromolecules by Suppression of Spin Diffusion.- Discussion.- NMR of Symmetrical Assemblies of Self-Recognizing Oligonucleotides.- Discussion.- Protein-DNA Interaction from NMR and Monte Carlo Docking.- Discussion.- Dynamic Structure of Nucleic Acid Duplexes.- Discussion.- Panel Discussion on Extension of Techniques to Larger Molecules.- NMR Structures of Proteins Involved in Signal Transduction.- Discussion.- Structures of Multimeric Proteins by NMR.- Discussion.- NMR Structural Studies of Flexible Molecules.- Iron-Sulfur Proteins: Investigations of Hyperfine-Shifted Hydrogen, Carbon, and Nitrogen Resonances.- On the Use of NMR in Complex Biological Systems: NMR Studies of Calcium Sensitive Interactions amongst Muscle Proteins.- Discussion.- The Structure of Lentiviral Tat Proteins in Solution.- Discussion.- A StructuralBiologist’s View of Precision and Accuracy of Structural Models of Proteins Based on NMR Data.- Discussion.- Panel Discussion on NMR vis-à-vis Other Structural Methods.- Poster Abstracts.