Time-resolved spectroscopy of wild-type and mutant Green Fluorescent Proteins reveals excited state deprotonation consistent with fluorophore-protein interactions
Authors:
- 1 December 1996
- journal article
- Published by Elsevier in Chemical Physics
- Vol. 213 (1-3) , 1-16
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Structure and fluorescence mechanism of GFPNature Biotechnology, 1996
- Crystal Structure of the Aequorea victoria Green Fluorescent ProteinScience, 1996
- PrefaceGene, 1996
- Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent proteinGene, 1996
- Chemistries and colors of bioluminescent reactions: a reviewGene, 1996
- FACS-optimized mutants of the green fluorescent protein (GFP)Gene, 1996
- Inhomogeneity of Radical Pair Energies in Photosynthetic Reaction Centers Revealed by Differences in Recombination Dynamics of P+HA- When Detected in Delayed Emission and in AbsorptionThe Journal of Physical Chemistry, 1994
- Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent proteinBiochemistry, 1993
- REVERSIBLE PHOTOCHEMISTRY IN THE α‐SUBUNIT OF PHYCOERYTHROCYANIN: CHARACTERIZATION OF CHROMOPHORE AND PROTEIN BY MOLECULAR DYNAMICS AND QUANTUM CHEMICAL CALCULATIONSPhotochemistry and Photobiology, 1993
- Primary structure of the Aequorea victoria green-fluorescent proteinGene, 1992