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).
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. Guéron 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. Rösch et al.). A Structural Biologist's View of Precision and Accuracy of Structural Models ofProteins Based on NMR Data (A.J. Wand). NMR vis á vis Other Structural Methods (B. Brooks et al.). Index.
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