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- Smith, Mackenzie A.; Phillips, Whitney K.; Rabin, Perry L.; Johnson, R. Jeremy
- Biochimica et biophysica acta 2018 v.1866 no.9 pp. 925-932
- Francisella tularensis; Gram-negative bacteria; active sites; alanine; bioactive properties; catalytic activity; electrostatic interactions; hydrophobicity; models; serine; serine proteinases; tryptophan
- ... The bacterial acyl protein thioesterase (APT) homologue FTT258 from the gram-negative pathogen Francisella tularensis exists in equilibrium between a closed and open state. Interconversion between these two states is dependent on structural rearrangement of a dynamic loop overlapping its active site. The dynamics and structural properties of this loop provide a simple model for how the catalytic a ...
- Glaves, John Paul; Ladner-Keay, Carol L.; Bjorndahl, Trent C.; Wishart, David S.; Sykes, Brian D.
- Biochimica et biophysica acta 2018 v.1866 no.9 pp. 982-988
- animal models; brain; disease course; neurodegenerative diseases; nuclear magnetic resonance spectroscopy; prion diseases; prions; proteinases; toxicity
- ... Prion (PrP) diseases are neurodegenerative diseases characterized by the formation of β-sheet rich, insoluble and protease resistant protein deposits (called PrPSᶜ) that occur throughout the brain. Formation of synthetic or in vitro PrPSᶜ can occur through on-pathway toxic oligomers. Similarly, toxic and infectious oligomers identified in cell and animal models of prion disease indicate that solub ...