In situ studies of protein conformation in supercritical fluids: Trypsin in carbon dioxide

Journal Article · Tue Sep 01 04:00:00 EDT 1992 · Biotechnology Progress

DOI:https://doi.org/10.1021/bp00017a008· OSTI ID:598195

Zagrobelny, J; Bright, F V ^[1]

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1. State Univ. of New York, Buffalo, NY (United States)

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{sub 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. 31 refs., 2 figs.

• Sponsoring Organization: USDOE
• DOE Contract Number: FG02-90ER14143
• OSTI ID: 598195
• Journal Information: Biotechnology Progress, Journal Name: Biotechnology Progress Journal Issue: 5 Vol. 8; ISSN BIPRET; ISSN 8756-7938
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
54 ENVIRONMENTAL SCIENCES
55 BIOLOGY AND MEDICINE
BASIC STUDIES
CARBON DIOXIDE
CONFORMATIONAL CHANGES
DENSITY
DYNAMICS
ENHANCED RECOVERY
ENZYME ACTIVITY
EXTRACTION CHROMATOGRAPHY
FLUIDS
FLUORESCENCE SPECTROSCOPY
MOLECULAR STRUCTURE
PHYSICAL PROPERTIES
PROTEIN DENATURATION
STABILITY
STEADY-STATE CONDITIONS
STRUCTURE-ACTIVITY RELATIONSHIPS
SUPERCRITICAL STATE
TRYPSIN
TURBULENT FLOW