In Situ Studies of Protein Conformation in Supercritical Fluids: Trypsin in Carbon Dioxide | Zendy

Zagrobelny Joann | Zendy; Bright Frank V. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

In Situ Studies of Protein Conformation in Supercritical Fluids: Trypsin in Carbon Dioxide

Author(s) -

Zagrobelny Joann,

Bright Frank V.

Publication year - 1992

Publication title -

biotechnology progress

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.572

H-Index - 129

eISSN - 1520-6033

pISSN - 8756-7938

DOI - 10.1021/bp00017a008

Subject(s) - trypsin , supercritical fluid , supercritical carbon dioxide , chemistry , denaturation (fissile materials) , carbon dioxide , fluorescence spectroscopy , in situ , fluorescence , monomer , native state , crystallography , biophysics , enzyme , biochemistry , organic chemistry , nuclear chemistry , biology , physics , polymer , quantum mechanics

The conformation of the monomeric enzyme trypsin has been studied in supercritical carbon dioxide. Steady‐state fluorescence spectroscopy is used to follow the conformation of trypsin in situ as a function of CO 2 density. Our results show for the first time that protein denaturation can occur during the fluid compression step and that the native trypsin is only slightly more stable (1.2 kcal/mol) than the unfolded form. These results demonstrate the power of fluorescence spectroscopy as a tool for studying protein conformation and dynamics in supercritical fluids.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research