The origin of the low steady-state fluorescence quantum yield of some blue-emitting variants of the green fluorescent protein (GFP) is investigated in single-site mutants in which the tyrosine residue at position 66 has been replaced by phenylalanine or by histidine. Time-resolved fluorescence measu
Picosecond Time-Resolved FRET in the Fluorescent Protein from Discosoma Red (wt-DsRed)
✍ Scribed by Tanja A. Schüttrigkeit; Ulrich Zachariae; Till von Feilitzsch; Jens Wiehler; Julia von Hummel; Boris Steipe; Maria E. Michel-Beyerle
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 87 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1439-4235
No coin nor oath required. For personal study only.
✦ Synopsis
Ultrafast, intra-oligomer fluorescence resonance energy transfer (FRET) between an immature green-emitting GFP-like chromophore to the mature red-emitting chromophore is found in the novel red fluorescent protein wt-DsRed (the picture shows the steady-state absorption (solid line) and emission (dotted) spectra). Since FRET is by its very nature a short range process, it represents a highly suitable method to probe oligomerization. This work describes a method preferentially applicable to the efficient screening of protein variants with mutagenetically altered surface docking sites.
📜 SIMILAR VOLUMES
LIMITING RELAXATION RATES IN THE STATISTICAL LIMIT .~\n intcnsc. tunable picusecond laser scurce hs been used for sckctivc excitation of vibronic bsnds of pe&cne in jrficprunc crysr;lls ncilr 4 K. 3leasurernents ofreson~ncc Iluoresccncc signals show relssttion times to have limiting vnlucs near 45 p