Current protocols in protein science / editorial board, John E. Coligan ... [et al.] 2013-01-01

Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes.

Guillaume Roussel, Emmanuel Tinti, Eric Perpète, Catherine Michaux

文献索引：Curr. Protoc. Protein Sci. Chapter 28 , Unit28.5, (2013)

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摘要

Currently, the investigation of protein refolding processes involves several time-consuming stages that require large amounts of protein and costly chemicals. Consequently, there is great interest in developing new approaches to the study of protein renaturation that are more technically and economically feasible. It has recently been reported that certain cosolvents are able to modulate the denaturing properties of sodium dodecyl sulfate (SDS) and induce the refolding of proteins. This unit presents a protocol to study and follow the renaturation of a protein (membrane or soluble) starting from a native or SDS-unfolded state using a variety of candidate cosolvents and osmolytes.

相关化合物

  • 十二烷基硫酸钠
  • 异己二醇
  • 溶菌酶,鸡蛋白
  • 溶菌酶
  • 氯化溶菌酶晶体
  • 溶菌酶

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