5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin
Visser, N.V. and Westphal, A.H. and Nabuurs, S.M. and van Hoek, A. and van Mierlo, C.P.M. and Visser, A.J.W.G. and Broos, J. and van Amerongen, H. (2009) 5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin. FEBS Letters, 583 (17). pp. 2785-2788. ISSN 0014-5793 (http://dx.doi.org/10.1016/j.febslet.2009.07.022)
Full text not available in this repository.Request a copyAbstract
The apoflavodoxin protein from Azotobacter vinelandii harboring three tryptophan (Trp) residues, was biosynthetically labeled with 5-fluorotryptophan (5-FTrp). 5-FTrp has the advantage that chemical differences in its microenvironment can be sensitively visualized via F-19 NMR. Moreover, it shows simpler fluorescence decay kinetics. The occurrence of FRET was earlier observed via the fluorescence anisotropy decay of WT apoflavodoxin and the anisotropy decay parameters are in excellent agreement with distances between and relative orientations of all Trp residues. The anisotropy decay in 5-FTrp apoflavodoxin demonstrates that the distances and orientations are identical for this protein. This work demonstrates the added value of replacing Trp by 5-FTrp to study structural features of proteins via F-19 NMR and fluorescence spectroscopy.
-
-
Item type: Article ID code: 18956 Dates: DateEvent3 September 2009PublishedSubjects: Science > Chemistry
Science > PhysicsDepartment: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Depositing user: Strathprints Administrator Date deposited: 10 Jun 2010 14:23 Last modified: 24 May 2024 01:42 URI: https://strathprints.strath.ac.uk/id/eprint/18956