Shedding light on ultrafast ring-twisting pathways of halogenated GFP chromophores from the excited to ground state

Author(s):  
Sean Boulanger ◽  
Cheng Chen ◽  
Longteng Tang ◽  
Liangdong Zhu ◽  
Nadezhda S. Baleeva ◽  
...  

Since green fluorescent protein (GFP) has revolutionized molecular and cellular biology for about three decades, there has been a keen interest in understanding, designing, and controlling the fluorescence properties of...

2004 ◽  
Vol 108 (21) ◽  
pp. 4587-4598 ◽  
Author(s):  
Mikas Vengris ◽  
Ivo H. M. van Stokkum ◽  
Xiang He ◽  
Alasdair F. Bell ◽  
Peter J. Tonge ◽  
...  

RSC Advances ◽  
2014 ◽  
Vol 4 (51) ◽  
pp. 26543-26551 ◽  
Author(s):  
Baotao Kang ◽  
Hongguang Liu ◽  
Du-Jeon Jang ◽  
Jin Yong Lee

In this paper, first-principles calculations were performed regarding the electric field effect on the ground state proton transfer (GSPT) in the H-bonded p-hydroxybenzylideneimidazolidinone (HBDI) network that represents the active site of the green fluorescent protein (GFP).


Tetrahedron ◽  
2015 ◽  
Vol 71 (30) ◽  
pp. 4987-4998 ◽  
Author(s):  
Masahiro Ikejiri ◽  
Kousuke Matsumoto ◽  
Hiraku Hasegawa ◽  
Daisuke Yamaguchi ◽  
Moe Tsuchino ◽  
...  

2020 ◽  
Author(s):  
Falk Schneider ◽  
Christian Eggeling ◽  
Erdinc Sezgin

SummaryAdvanced fluorescence microscopy studies require specific and monovalent molecular labelling with bright and photostable fluorophores. This necessity led to the widespread use of fluorescently labelled nanobodies against commonly employed fluorescent proteins. However, very little is known how these nanobodies influence their target molecules. Here, we observed clear changes of the fluorescence properties, mobility and organisation of green fluorescent protein (GFP) tagged proteins after labelling with an anti-GFP nanobody. Intriguingly, we did not observe any co-diffusion of fluorescently-labelled nanobodies with the GFP-labelled proteins. Our results suggest significant binding of the nanobodies to a non-emissive, oligomerized form of the fluorescent proteins, promoting disassembly into more monomeric forms after binding. Our findings show that great care must be taken when using nanobodies for studying dynamic and quantitative protein organisation.


Biochemistry ◽  
2014 ◽  
Vol 53 (37) ◽  
pp. 5947-5957 ◽  
Author(s):  
Luke M. Oltrogge ◽  
Quan Wang ◽  
Steven G. Boxer

2000 ◽  
Vol 104 (19) ◽  
pp. 4791-4798 ◽  
Author(s):  
Andreas D. Kummer ◽  
Jens Wiehler ◽  
Hermann Rehaber ◽  
Christian Kompa ◽  
Boris Steipe ◽  
...  

FEBS Letters ◽  
2003 ◽  
Vol 549 (1-3) ◽  
pp. 35-38 ◽  
Author(s):  
Xiang He ◽  
Alasdair F. Bell ◽  
Peter J. Tonge

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