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The mechanism of folding robustness revealed by the crystal structure of extra‐superfolder GFP
Author(s) -
Choi Jae Young,
Jang TaeHo,
Park Hyun Ho
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12534
Subject(s) - green fluorescent protein , robustness (evolution) , mutagenesis , protein folding , biophysics , protein stability , chemistry , protein engineering , microbiology and biotechnology , biology , mutation , biochemistry , gene , enzyme
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.