| Literature DB >> 9169619 |
S D'auria1, R Barone, M Rossi, R Nucci, G Barone, D Fessas, E Bertoli, F Tanfani.
Abstract
The effects of temperature and SDS on the three-dimensional organization and secondary structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus were investigated by CD, IR spectroscopy and differential scanning calorimetry. CD spectra in the near UV region showed that the detergent caused a remarkable change in the protein tertiary structure, and far-UV CD analysis revealed only a slight effect on secondary structure. Infrared spectroscopy showed that low concentrations of the detergent (up to 0.02%) induced slight changes in the enzyme secondary structure, whereas high concentrations caused the alpha-helix content to increase at high temperatures and prevented protein aggregation.Entities:
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Year: 1997 PMID: 9169619 PMCID: PMC1218389 DOI: 10.1042/bj3230833
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857