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Subtilisin enzymes: A note on time‐resolved fluorescence and circular dichroism properties
Author(s) -
Bayley P.M.,
Janot J.-M.,
Martin S.R.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80762-8
Subject(s) - subtilisin , circular dichroism , fluorescence , chemistry , crystallography , biophysics , enzyme , biochemistry , biology , optics , physics
This note briefly corrects previous information about the time‐resolved fluorescence properties of preparations of subtilisin Carlsberg and subtilisin BPN′. We confirm the observation of segmental motion of the single tryptophan in subtilisin Carlsberg by analysis of the time‐resolved fluorescence anisotropy, and present circular dichroism and spectroscopic data on the two proteins. Near‐UV properties clearly differentiate between the two proteins. Far‐UV circular dichroism confirms that the two subtilisins have closely similar secondary structure in solution; the multi‐component analysis is consistent with the established X‐ray conformations, but the quantitative agreement is still somewhat imperfect.