Effects of temperature and SDS on the structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus.
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.
D'auria
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Istituto di Biochimica delle Proteine ed Enzimologia, C.N.R., Via Marconi 10, 80125 Napoli, Italia.
Barone
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Rossi
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M
Nucci
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R
Barone
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G
Fessas
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D
Bertoli
E
E
Tanfani
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F
D001426:Bacterial Proteins / Q000737:chemistry* / Q000187:drug effects; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003902:Detergents / Q000494:pharmacology*; D005959:Glucosidases / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013055:Spectrophotometry, Infrared; D016944:Sulfolobus / Q000201:enzymology* / Q000502:physiology; D013696:Temperature
D001426:Bacterial Proteins; D003902:Detergents; D012967:Sodium Dodecyl Sulfate; D005959:Glucosidases; C104851:Sulfolobus solfataricus beta-glycosidase