Electronic spectroscopy and solvatochromism in the chromophore of GFP and the Y66F mutant

被引：33

作者：

Webber, Naomi M. ^{[1
]}

Meech, Stephen R. ^{[1
]}

机构：

[1] Univ E Anglia, Sch Chem Sci & Pharm, Norwich NR4 7TJ, Norfolk, England

来源：

PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES | 2007年 / 6卷 / 09期

关键词：

D O I：

10.1039/b707578b

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 electronic spectra of the chromophore of the wild type green fluorescent protein, GFP, and of a mutant form Y66F GFP in which the chromophore lacks the hydroxyl group have been studied. The acid-base properties, solvatochromism, vibronic structure and edge excitation red shift have all been measured. The results are compared with the spectra of the chromophore in the protein environment. These data suggest that the transition energy for the GFP chromophore is in fluenced by a number of factors in its environment, and in particular by hydrogen bonding.

引用

页码：976 / 981

页数：6

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