Arakawa Tsutomu, Yamaguchi Rui, Tokunaga Hiroko, Tokunaga Masao
Alliance Protein Laboratories, 6042 Cornerstone Court West, Suite A, San Diego, CA 92121, USA.
Curr Protein Pept Sci. 2017;18(1):65-71. doi: 10.2174/1389203717666160617111140.
Proteins from moderate and extreme halophiles have unique characteristics. They are highly acidic and hydrophilic, similar to intrinsically disordered proteins. These characteristics make the halophilic proteins soluble in water and fold reversibly. In addition to reversible folding, the rate of refolding of halophilic proteins from denatured structure is generally slow, often taking several days, for example, for extremely halophilic proteins. This slow folding rate makes the halophilic proteins a novel model system for folding mechanism analysis. High solubility and reversible folding also make the halophilic proteins excellent fusion partners for soluble expression of recombinant proteins.
来自中度嗜盐菌和极端嗜盐菌的蛋白质具有独特的特性。它们高度酸性且亲水性强,类似于内在无序蛋白。这些特性使嗜盐蛋白可溶于水并能可逆折叠。除了可逆折叠外,嗜盐蛋白从变性结构重新折叠的速率通常较慢,例如对于极端嗜盐蛋白,往往需要几天时间。这种缓慢的折叠速率使嗜盐蛋白成为用于折叠机制分析的新型模型系统。高溶解性和可逆折叠也使嗜盐蛋白成为重组蛋白可溶性表达的优秀融合伙伴。