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• W2052207497 abstract "To facilitate the process of protein design and learn the basic rules that control the structure and stability of proteins, combinatorial methods have been developed to select or screen proteins with desired properties from libraries of mutants. One such method uses phage-display and proteolysis to select stably folded proteins. This method does not rely on specific properties of proteins for selection. Therefore, in principle it can be applied to any protein. Since its first demonstration in 1998, the method has been used to create hyperthermophilic proteins, to evolve novel folded domains from a library generated by combinatorial shuffling of polypeptide segments and to convert a partially unfolded structure to a fully folded protein." @default.
• W2052207497 created "2016-06-24" @default.
• W2052207497 creator A5069137667 @default.
• W2052207497 creator A5072545375 @default.
• W2052207497 date "2004-05-01" @default.
• W2052207497 modified "2023-09-26" @default.
• W2052207497 title "Selection of stably folded proteins by phage-display with proteolysis" @default.
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• W2052207497 doi "https://doi.org/10.1111/j.1432-1033.2004.04074.x" @default.
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