Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Choi JY,Jang TH,Park HHdoi
10.1002/1873-3468.12534subject
Has Abstractpub_date
2017-01-01 00:00:00pages
442-447issue
2eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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