A 500 MHz NMR spectrometer and computer system will be acquired for use in structural biology. New software will be developed for analyzing NMR data and utilizing that data to determine the structure of proteins in solution. Additional studies concern the relationship between the linear or primary sequence of proteins and the secondary and tertiary fording of proteins in three dimensional space. NMR data will be used to evaluate schemes for understanding the potential conformations of identical sequences of amino acids contained in different larger amino acid sequences. The structure and dynamics of short DNA oligomeric chains and of small molecules that interact with DNA and protein will also be studied. The information derived from the NMR experiments will be used in conjunction with distance geometry calculations, energy refinement calculations and computer graphics to generate molecular structures in solution in greater detail than is presently known. The information will be compared to our knowledge of the static structure of proteins and DNA known from X-ray diffraction data, and will lead to a better understanding of the relationship between architecture and the functional role of these macromolecules.
