Time-resolved emission spectra of green fluorescent protein

被引：17
|
作者：
Jaye, AA
Stoner-Ma, D
Matousek, P
Towrie, M
Tonge, PJ
Meech, SR [1 ]
机构：
[1] Univ E Anglia, Sch Cem Sci & Pharm, Norwich NR4 7TJ, Norfolk, England
[2] SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA
[3] Rutherford Appleton Lab, CCLRC, Cent Laser Facil, Didcot OX11 0QX, Oxon, England
来源：
PHOTOCHEMISTRY AND PHOTOBIOLOGY | 2006年 / 82卷 / 02期
关键词：
D O I：
10.1562/2005-05-07-RA-518
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The time-resolved emission spectra of wild-type green fluorescent protein (wtGFP) and the T203V GFP mutant have been recorded with picosecond time resolution, allowing the separate characterization of the two spectral components associated with the neutral and anionic forms of the GFP chromophore. Significantly, neither component shifts as a function of time. It is suggested that the absence of spectral shift is a result of highly restricted movement of the protein residues in the vicinity of the chromophore. The shapes of the separated spectra are discussed and their relative ratio analyzed in a steady-state analysis.
引用
收藏
页码：373 / 379
页数：7
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