Protein Dynamics of the Sensor Protein HemAT as Probed by Time-Resolved Step-Scan FTIR Spectroscopy.

ABSTRACT: The heme-based aerotactic transducer (HemAT) is an oxygen-sensor protein consisting of a sensor and a signaling domain in the N- and C-terminal regions, respectively. Time-resolved step-scan FTIR spectroscopy was employed to characterize protein intermediate states obtained by photolysis of the carbon monoxide complexes of sensor-domain, full-length HemAT, and the Y70F (B-helix), L92A (E-helix), T95A (E-helix), and Y133F (G-helix) HemAT mutants. We assign the spectral components to discrete substructures, which originate from a helical structure that is solvated (1638 cm^-1) and a native helix that is protected from solvation by interhelix tertiary interactions (1654 cm^-1). The full-length protein is characterized by an additional amide I absorbance at 1661 cm^-1</

SUBMITTER: Pavlou A 

PROVIDER: S-EPMC5985031 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature