|
KMID : 1094720160210060720
|
|
Biotechnology and Bioprocess Engineering
2016 Volume.21 No. 6 p.720 ~ p.725
|
|
|
Single amino acid replacement transforms mCherry to a far-red fluorescent protein
|
|
Kim Ye-Ji
Song Kyung-Ju
Lee Hwa-Jin
Kim Do-Hyun
Kim Jin-Tae
Chung Min-Sub
|
|
|
Abstract
|
|
|
|
Far-red fluorescent proteins are beneficial for imaging in mammals. Here, starting from mCherry, the most commonly used among the different types of red fluorescent proteins (RFP), not having a H-bond network in its original form, we sought to recover the hydrogen bond network in mCherry. By comparing the structure of wtGFP and mCherry, we focused on a few key residues involved in a proton wire, and discovered an I197T mutant that showed a more red-shifted fluorescence. The detailed optical and photo-switching properties of related engineered RFPs are described. This study will guide further development of monomeric far-red FPs.
|
|
|
KEYWORD
|
|
|
far-red fluorescent proteins, mCherry, mutagenesis
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
 
|