| Autor: |
Matthew R. Anderson, Caitlin M. Padgett, Victoria O. Ogbeifun, Natasha M. DeVore |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
SynBio, Vol 2, Iss 3, Pp 298-310 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2674-0583 |
| DOI: |
10.3390/synbio2030018 |
| Popis: |
Thermal green protein Q66E (TGP-E) has previously shown increased thermal stability compared to thermal green protein (TGP), a thermal stable fluorescent protein produced through consensus and surface protein engineering. In this paper, we describe the protein crystal structure of TGP-E to 2.0 Å. This structure reveals alterations in the hydrogen bond network near the chromophore that may result in the observed increase in thermal stability. We compare the very stable TGP-E protein to the structure of a yellow mutant version of this protein YTP-E E148D. The structure of this mutant protein reveals the rationale for the observed low quantum yield and directions for future protein engineering efforts. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
