Abstract
ABSTRACT High pressure circular dichroism (HP-CD) spectroscopy below 200 MPa, especially in the near-ultraviolet region, has long been expected to probe the protein self-association phenomena. However, its experimental difficulties have hampered obtaining the data available for quantitative analyses. In this paper, near-ultraviolet CD spectra measurements under various temperatures and pressures were demonstrated on nitrilase from Rhodococcus rhodochrous J1 (J1-NTase), which thermally self-associates from inactive protomer to active oligomer at atmospheric pressure. The exploration of instrumental conditions and simple raw data correction enabled us to complete the spectra in a temperature-pressure plane. The quality of data was checked by multivariate curve resolution with the alternating least squares method (MCR-ALS), which gave model-free decomposition into component spectra and their concentration profiles. The resultant two components pointed out that the obtained data were self-consistent and appeared to reflect free and bound protomers.
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