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Selection based on the folding properties of proteins with ribosome display
Author(s) -
Matsuura Tomoaki,
Plückthun Andreas
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00178-9
Subject(s) - folding (dsp implementation) , proteolysis , protein folding , random coil , selection (genetic algorithm) , computational biology , directed molecular evolution , chemistry , ligand (biochemistry) , ribosome , biophysics , biology , biochemistry , directed evolution , computer science , protein secondary structure , rna , receptor , mutant , gene , electrical engineering , enzyme , engineering , artificial intelligence
Ribosome display is a powerful tool for selecting and evolving protein functions through ligand‐binding. Here, this in vitro system was used to perform selection based on the folding properties of proteins, independent of specific ligand‐binding. The selection is based on two properties of misfolded proteins: (1) increased sensitivity to proteolysis and (2) greater exposure of hydrophobic area. By targeting these properties, we show that compactly folded and soluble proteins can be enriched over insoluble and random coil proteins. This approach may be especially useful for selection and evolution of folded proteins from random sequence libraries.