TAILIEUCHUNG - Báo cáo khoa học: Selection of stably folded proteins by phage-display with proteolysis

To facilitate the process of proteindesign 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 proteo-lysis to select stably folded proteins. This method does not rely on specific properties of proteins for selection. There-fore, 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 froma librarygeneratedby combinatorial shuffling of polypeptide segments and to convert a partially unfolded structure to a fully folded protein | Eur. J. Biochem. 271 1609-1614 2004 FEBS 2004 doi MINIREVIEW Selection of stably folded proteins by phage-display with proteolysis Yawen Bai and Hanqiao Feng Laboratory of Biochemistry National Cancer Institute Bethesda MD USA 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. Keywords hydrophobic repacking phage-display protein design proteolysis. Introduction There are two basic biophysical issues in protein design. One is to find mutations that make proteins thermodynamically more stable. The other is to find an amino acid sequence for a polypeptide chain that will fold to a target structure. The first issue is important for developing therapeutic drugs and useful enzymes in industry. The second issue is more critical for learning and testing the principles of protein folding. Although significant progress has been made towards rational design of proteins with simple motifs 1-3 it is still difficult to design native-like proteins with globular structures 4 . In addition it is still not completely clear how the stability of a protein is encoded in the protein s sequence and how individual amino acid residues contribute to stability. Thus combinatorial approaches to select or screen proteins with the desired properties from libraries of mutant proteins

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