Akira Naito , Yokohama National University, 79-5 Tokiwadai, Hodogaya-ku,, Yokohama, JP, 240-8501 | Ayyalusamy Ramamoorthy | Frances Separovic | M. Auger

Solid-state NMR is a powerful tool for elucidating structure-function relationships at atomic resolution in a variety of biological systems. As an approach of structural biology, recoupling methods solid-state NMR spectroscopy have greatly progressed to determine interatomic distances of site specific and uniformly labeled biomolecules. This distance information together with chemical shift interactions are used as structural constraints for determining the three-dimensional structure of solid biological macromolecules. Solid-state NMR can also provide molecular images based on orientational information in mechanically and magnetically ordered systems of biomolecules such as membrane proteins and peptides, including antimicrobial peptides, fusion peptides, toxins and ion channels. Unique information about dynamics can be obtained in the solid-state or in membranes since local motions can be studied without the complexity of overall tumbling over a wide range of time scales, which are relevant to biological function. The following topics will be discussed in this symposium: (i) technical developments in resolution and sensitivity enhancements of solid-state NMR; (ii) high-resolution structure determination of biomolecules by solid-state NMR; (iii) advances in structural biology of membrane proteins and peptides; (iv) dynamics and biomolecular function by solid-state NMR; and (v) characterization of supramolecular complexes and fibril-forming proteins.