Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
226867 | Journal of Industrial and Engineering Chemistry | 2016 | 6 Pages |
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.
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Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Bharat Madan, Jayaraman Thangappan, Sun-Gu Lee,