This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Computing at the Pittsburgh Supercomputing CenterCurrent computational advances for biomolecular NMR make it possible to do structure calculation automatically from assigned chemical shifts without any manual interpretation of spectra (1,2). I have successfully used these techniques for the calculation of several protein structures (3-6). In addition, for the calculation of homo multimeric protein structure, I extended current algorithm to consider NOEassignment degeneracy as well. To use these algorithms efficiently, however, extensive computations are needed. I will use systems of PSC to calculate GB1 mutants which form dimer or tetramer. By changing core residues, small, stable, and monomeric protein GB1 is converted into multimers (7-9). The algorithm which combines NOE network anchoring of CANDID/CYANA package (1) and empirical force terms of XPLOR_NIH package (10) will be applied to calculate the structures of these mutants in an automatic manner. Furthermore, I have a plan todo MD simulation of these mutants to understand their dynamic characters.
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