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- W2016221452 abstract "A type I beta-turn in green fluorescent protein (GFP) was engineered to a foreign loop. Molecular dynamics simulation study showed that the addition of foreign loop into GFP did not have a negative influence on the conformation stability of GFP structure, but the GFP variant with the foreign loop sequence was completely misfolded in real folding conditions. The co-incorporation of the enhancing mutations for GFP folding made it possible to generate a foldable and active GFP variant with the foreign loop sequence, although the folding efficiency and specific activity of the GFP were negatively affected by the introduced loop." @default.
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- W2016221452 date "2007-01-01" @default.
- W2016221452 modified "2023-10-14" @default.
- W2016221452 title "Conformational analysis of compstatin analogues with molecular dynamics simulations in explicit water" @default.
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- W2016221452 doi "https://doi.org/10.1016/j.molimm.2006.07.013" @default.
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