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Folding & Design|January 1, 1997
Estimates for the potential accuracy required in realistic protein folding simulations and structure recognition experimentsA F de Araújo, T C PochapskyProtein Science : a Publication of the Protein Society|June 1, 1992
A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chainsT C Pochapsky, Q GopenJournal of Biomolecular NMR|June 1, 1997
Structural features of the metal binding site and dynamics of gallium putidaredoxin, a diamagnetic derivative of a Cys4Fe2S2 ferredoxinS Kazanis, T C PochapskyCurrent Topics in Medicinal Chemistry|March 20, 2002
Nuclear magnetic resonance as a tool in drug discovery, metabolism and dispositionS S Pochapsky, T C PochapskyBiochemical and Biophysical Research Communications|May 1, 1999
A new assignment strategy for the hyperfine-shifted 13C and 15N resonances in Fe2S2 ferredoxinsN U Jain, T C PochapskyBiochemistry|April 23, 1991
1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxinT C Pochapsky, X M YeFolding & Design|January 1, 1996
Monte Carlo simulations of protein folding using inexact potentials: how accurate must parameters be in order to preserve the essential features of the energy landscape?A F Pereira de Araújo, T C PochapskyJournal of Biomolecular NMR|December 3, 1998
The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85ST C Pochapsky, M Kuti, S KazanisBiochemistry|May 31, 1994
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxinT C Pochapsky, G Ratnaswamy, A PateraBiochemistry|May 24, 2001
Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniaeY Dai, T C Pochapsky, R H AbelesPageof 3