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.
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.
