Jackson Sophie E, Craggs Timothy D, Huang Jie-rong
Chemistry Department, Lensfield Road, Cambridge CB2 1EW, UK.
Expert Rev Proteomics. 2006 Oct;3(5):545-59. doi: 10.1586/14789450.3.5.545.
Green fluorescent protein (GFP) and its many variants are probably the most widely used proteins in medical and biological research, having been extensively engineered to act as markers of gene expression and protein localization, indicators of protein-protein interactions and biosensors. GFP first folds, before it can undergo an autocatalytic cyclization and oxidation reaction to form the chromophore, and in many applications the folding efficiency of GFP is known to limit its use. Here, we review the recent literature on protein engineering studies that have improved the folding properties of GFP. In addition, we discuss in detail the biophysical work on the folding of GFP that is beginning to reveal how this large and complex structure forms.
绿色荧光蛋白（GFP）及其众多变体可能是医学和生物学研究中使用最广泛的蛋白质，它们经过广泛改造后可作为基因表达和蛋白质定位的标记、蛋白质-蛋白质相互作用的指标以及生物传感器。GFP首先折叠，然后才能进行自催化环化和氧化反应以形成发色团，并且在许多应用中，已知GFP的折叠效率会限制其使用。在这里，我们综述了有关改善GFP折叠特性的蛋白质工程研究的最新文献。此外，我们详细讨论了关于GFP折叠的生物物理研究，这些研究开始揭示这种大型复杂结构是如何形成的。
