Abstract
Fluorescence techniques were used to study conformational changes in UDPgalactose:lipopolysaccharide alpha,3-galactosyltransferase (EC 2.4.1.44). Intramolecular energy transfer was measured from the single tryptophan residue in the peptide to a pyridoxal phosphate group linked to the same peptide via a reduced Schiff's base. Significant differences in energy transfer were seen when the enzyme was studied in aqueous solution and after entry into a phospholipid-lipopolysaccharide matrix, paralleling the restoration of its catalytic activity. Further differences were seen when the structures of the phospholipids and lipopolysaccharides were changed. Application of the Förster theory indicated that the changes in energy transfer resulted from changes in distances between the chromophores and/or changes in their relative orientations. The results suggest that entry of this membrane protein into a lipid matrix induces a change in conformation of the protein and that other alternative conformations can be induced by further changes in its lipid environment.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
