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Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. Volume 16, with the subtitle Modern Techniques in Protein NMR , is the first in this series. These two volumes present some of the recent, significant advances in the biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volume some of the world s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains - vances in two broad categories: I. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.
Section I: Computational Methods. 1. Aspects of Modeling Biomolecular Structure on the Basis of Spectroscopic or Diffraction Data; W.F. van Gunsteren, et al. 2. Combined Automated Assignment of NMR Spectra and Calculation of Three-dimensional Protein Structures; Yuan Xu, et al. 3. NMR Pulse Sequences and Computational Approaches for Automated Analysis of Sequence-Specific Backbone Resonance Assignments of Proteins; G.T. Montelione, et al. 4. Calculation of Symmetric Oligomer Structures from NMR Data; S.I. O'Donoghue, M. Nilges. 5. Hybrid-Hybrid Matrix Method for 3D NOESY-NOESY Data Refinements; E.K. Gozansky, et al. 6. Conformational Ensemble Calculations: Analysis of Protein and Nucleic Acid NMR Data; A. Mujeeb, et al. 7. Complete Relaxation and Conformational Exchange Matrix (CORCEMA) Analysis of NOESY Spectra of Reversibly Forming Ligand-Receptor Complexes: Application to Transferred NOESY; N. Rama Krishna, H.N.B. Moseley. Section II: Structure and Dynamics. 8. Protein Structure and Dynamics from Field-Induced Residual Dipolar Couplings; J.H. Prestegard, et al. 9. Recent Developments in Studying the Dynamics of Protein Structures from 15N and 13C Relaxation Time Measurements; J. Engelke, H. Rüterjans. 10. Multinuclear Relaxation Dispersion Studies of Protein Hydration; B. Halle, et al. 11. Hydration Studies of Biological Macromolecules by Intermolecular Water-Solute NOEs; G. Otting. Contents of Previous Volumes. Index.