CONFERENCE ON FRONTIERS OF NMR IN MOLECULAR BIOLOGY VII

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DESCRIPTION (Applicant's Description) Nuclear Magnetic Resonance (NMR) is playing an increasingly important role in the determination of macromolecular Structures and the study of protein and nucleic acid dynamics. This growing importance of NMR in structural biology is powerfully illustrated by the number of novel structures of biological macromolecules determined by this technique over the last few years. For example, approximately 250 new NMR structures are deposited in the PDB each year, a remarkable number given the fact that the structural NMR field is still in the developing phase compared to the mature area of crystallography. In addition, a growing number of NMR groups have been established at universities, research institutions, and industry, reflecting the vigor of the field. But NMR is not only a technique for structure determination, it is also able to provide a wealth of information which is complementary to the structural data. NMR data on dynamics and solvation of proteins and nucleic acids is becoming available as well as NMR characterization of partially folded or infolded protein and polypeptide states. A major research goal is to increase the size of the protein or macromolecular complex that can be analyzed by NMR. This requires the development of even higher-field spectrometers, which will yield higher sensitivity and better resolution, thereby improving the quality of structures of all sizes. Hand in hand with these instrument developments will be methodological approaches to overcome or minimize the correlation time problem. Despite major advances, NMR data collection still represents a substantial investment in real time and in equipment time and may require several months for one structure. Avenues for increasing the number of NMR Structures are sought through high throughput approaches or streamlining experiments. NMR is one of very few techniques which will be able to provide structural and dynamical data on partially folded and heterogeneous protein systems, i.e. amyloids. Studies on these will have major implications for pathology and disease. The meeting will be the forum to present the newest structures of important proteins, nucleic acids and complexes thereof, illuminating key functional questions in molecular biology. Methodological and functional discussions will be given equal weight. The excitement about NMR is vividly appreciated from the NMR supplement of Nature Structural Biology, July 5, 1998 and a News and Views article in Science, 279,1127,1998