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An infrared spectroscopic study of β‐galactosidase structure in aqueous solutions
Author(s) -
Arrondo J.L.R.,
Muga A.,
Castresana J.,
Bernabeu C.,
Goñi F.M.
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)80901-9
Subject(s) - random coil , aqueous solution , protein secondary structure , infrared , fourier transform infrared spectroscopy , infrared spectroscopy , chemistry , fourier transform , analytical chemistry (journal) , spectral line , crystallography , sequence (biology) , physics , biochemistry , mathematics , optics , chromatography , organic chemistry , mathematical analysis , astronomy
Fourier‐transform infrared spectroscopy has been used to elucidate the secondary structure of E. coli β‐galactosidase in aqueous solution. The structure of this enzyme was previously unknown above the level of the amino acid sequence. Spectra have been recorded in both H 2 O and D 2 O media; mutually complementing data are obtained, that provide unambiguous structural information. The results show that β‐galactosidase contains 40% β‐sheet and 35% α‐helical structure, with smaller proportions of random coil (12%) and β‐turns (13%).