Single amino acid replacement transforms mCherry to a far-red fluorescent protein |
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Authors: | Yeji Kim Kyungju Song Hwajin Lee Dohyun Kim Jintae Kim Minsub Chung |
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Affiliation: | 1.Department of Chemical Engineering,Hongik University,Seoul,Korea;2.Department of Mechanical Engineering,Myongji University,Yongin,Korea;3.Department of Electronics Engineering,Konkuk University,Seoul,Korea |
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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. |
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