Structural highlights
Publication Abstract from PubMed
Stability of green fluorescent protein (GFP) is sometimes important for a proper practical application of this protein. Random mutagenesis and targeted mutagenesis have been used to create better-folded variants of GFP, including recently reported extra-superfolder GFP. Our aim was to determine the crystal structure of extra-superfolder GFP, which is more robustly folded and stable than GFP and superfolder GFP. The structural and structure-based mutagenesis analyses revealed that some of the mutations that created extra-superfolder GFP (F46L, E126K, N149K, and S208L) contribute to folding robustness by stabilizing extra-superfolder GFP with various noncovalent bonds.
The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP.,Choi JY, Jang TH, Park HH FEBS Lett. 2017 Jan;591(2):442-447. doi: 10.1002/1873-3468.12534. Epub 2016 Dec, 28. PMID:27990640[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Choi JY, Jang TH, Park HH. The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP. FEBS Lett. 2017 Jan;591(2):442-447. doi: 10.1002/1873-3468.12534. Epub 2016 Dec, 28. PMID:27990640 doi:http://dx.doi.org/10.1002/1873-3468.12534
