Thomas Szyperski, Ph.D. [http://www.chem.buffalo.edu/Szyperski.html]

University at Buffalo
Department of Chemistry
816 Natural Sciences Complex
Buffalo, NY  14260-3000
Phone: (716)645-6800 ext. 2245
Fax: (716) 645-6963
Email: szypersk@buffalo.edu

Research in the Szyperski group focuses on nuclear magnetic resonance (NMR) based structural genomics pursued in the framework of the Northeast Structural Genomics Consortium (NESGC; http://www.nesg.org). NESGC is one out of nine US consortia funded through the ‘Protein Structure Initiative’ (PSI) set forth by NIH.

Structural genomics aims at (i) the exploration of protein fold space and (ii) the support of the functional annotation of the human genome. The goal of objective (i) is to make at least one experimental protein structure at atomic resolution available for each family of sequence homologues. In turn, this shall than allow one to ‘homology model’ the structures of the other members of a given family.

Specifically, Szyperski’s group solves structures of protein targets of the NESGC (see, for example, Fig. 1) and develops methodology for rapid acquisition of multi-dimensional NMR data (for example, the recently introduced ‘G-matrix Fourier transform NMR spectroscopy’).

Fig. 1. A novel fold (protein architecture) found for the NESGC target protein encoded in gene YI57 of A. aeolicus (Duanxiang Xu, Gaohua Liu, Rong Xiao, Tom Acton, Sharon Goldsmith-Fischman, Barry Honig, Gaetano T. Montelione, Thomas Szyperski, 2004, Proteins, in press). A ribbon drawing of the structure is shown. a-helices I and II are shown in red and yellow, the b-strands A to G are in cyan, other polypeptide segments are in grey, and the N- and C-terminal ends of the protein are indicated as ‘N’ and ‘C’. (B) Same as in (A), but rotated by 90o about the vertical axis. a-Helix I: residues 14-25, II: 77-79; b-Strand A: 10-12, B: 33-36, C: 52-53, D: 63-65, E: 69-72, F: 84-89, G: 94-99.