The UvA-LINKER will give you a range of other options to find the full text of a publication (including a direct link to the full-text if it is located on another database on the internet).
De UvA-LINKER biedt mogelijkheden om een publicatie elders te vinden (inclusief een directe link naar de publicatie online als deze beschikbaar is in een database op het internet).
faculty: "FNWI" and publication year: "2004"
| Authors||M. Vengris, M.A. van der Horst, G. Zgrablic, I.H.M. van Stokkum, S. Haacke, M. Chergui, K.J. Hellingwerf, R. van Grondelle, D.S. Larsen|
|Title||Contrasting the excited-state dynamics of the photoactive yellow protein chromophore: Protein versus solvent environments.|
|Faculty||Faculty of Science|
|Institute/dept.||FNWI: Swammerdam Institute for Life Sciences (SILS)|
|Keywords||Bacterial Proteins; Fluorescence Microscopy; Photoactive yellow protein; Photoreceptors; Spectrophotometry|
|Classification||33.93 ; 35.73 ; 42.12 ; 42.15 |
|Abstract||Wavelength- and time-resolved fluorescence experiments have been performed on the photoactive yellow protein, the E46Q mutant, the hybrids of these proteins containing a nonisomerizing "locked" chromophore, and the native and locked chromophores in aqueous solution. The ultrafast dynamics of these six systems is compared and spectral signatures of isomerization and solvation are discussed. We find that the ultrafast red-shifting of fluorescence is associated mostly with solvation dynamics, whereas isomerization manifests itself as quenching of fluorescence. The observed multiexponential quenching of the protein samples differs from the single-exponential lifetimes of the chromophores in solution. The locked chromophore in the protein environment decays faster than in solution. This is due to additional channels of excited-state energy dissipation via the covalent and hydrogen bonds with the protein environment. The observed large dispersion of quenching timescales observed in the protein samples|
Use this url to link to this page: http://dare.uva.nl/en/record/148983
Contact us about this recordNotify a colleague
Add to bookbag