Single Amino Acid Replacement Transforms mCherry to a Far-red Fluorescent Protein
- Authors
- Kim, Yeji; Song, Kyungju; Lee, Hwajin; Kim, Dohyun; Kim, Jintae; Chung, Minsub
- Issue Date
- Nov-2016
- Publisher
- KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
- Keywords
- far-red fluorescent proteins; mCherry; mutagenesis
- Citation
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.21, no.6, pp.720 - 725
- Journal Title
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
- Volume
- 21
- Number
- 6
- Start Page
- 720
- End Page
- 725
- URI
- https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/7218
- DOI
- 10.1007/s12257-016-0402-3
- ISSN
- 1226-8372
- 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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Collections - College of Engineering > Chemical Engineering Major > 1. Journal Articles
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