Structural and Spectral Response of Green Fluorescent Protein Variants to Changes in pH†,‡

Biochemistry ◽  
1999 ◽  
Vol 38 (17) ◽  
pp. 5296-5301 ◽  
Author(s):  
Marc-André Elsliger ◽  
Rebekka M. Wachter ◽  
George T. Hanson ◽  
Karen Kallio ◽  
S. James Remington
Biochemistry ◽  
2005 ◽  
Vol 44 (24) ◽  
pp. 8701-8711 ◽  
Author(s):  
Tim B. McAnaney ◽  
Xinghua Shi ◽  
Paul Abbyad ◽  
Henry Jung ◽  
S. James Remington ◽  
...  

2001 ◽  
Vol 81 (S36) ◽  
pp. 117-128 ◽  
Author(s):  
Andrea Sacchetti ◽  
Valeria Cappetti ◽  
Pierfrancesco Marra ◽  
Roberta Dell'Arciprete ◽  
Tarek El Sewedy ◽  
...  

1998 ◽  
Vol 64 (6) ◽  
pp. 2240-2246 ◽  
Author(s):  
Jens Bo Andersen ◽  
Claus Sternberg ◽  
Lars Kongsbak Poulsen ◽  
Sara Petersen Bjørn ◽  
Michael Givskov ◽  
...  

ABSTRACT Use of the green fluorescent protein (Gfp) from the jellyfishAequorea victoria is a powerful method for nondestructive in situ monitoring, since expression of green fluorescence does not require any substrate addition. To expand the use of Gfp as a reporter protein, new variants have been constructed by the addition of short peptide sequences to the C-terminal end of intact Gfp. This rendered the Gfp susceptible to the action of indigenous housekeeping proteases, resulting in protein variants with half-lives ranging from 40 min to a few hours when synthesized in Escherichia coli andPseudomonas putida. The new Gfp variants should be useful for in situ studies of temporal gene expression.


Biochemistry ◽  
2002 ◽  
Vol 41 (52) ◽  
pp. 15477-15488 ◽  
Author(s):  
George T. Hanson ◽  
Tim B. McAnaney ◽  
Eun Sun Park ◽  
Marla E. P. Rendell ◽  
Daniel K. Yarbrough ◽  
...  

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