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文献和实验Screening Peptide/Protein Libraries Fused to the Repressor DNA-Binding Domain in E. coli Cells
to detect protein-protein interactions in vivo. Protein or peptide targets are fused to the λ repressor DNA binding domain; these fusions can be evaluated for repressor activity using direct selection with λ phage, or a variety of reporter genes suitable
Two dimensional peptide mapping
itself. Usually, 3-4 days exposure with a screen and flashed film is necessary to detect samples containing 100-200 cpm of 32P. Recipes for peptide mapping. It's sensible to make 2L
Mapping Protein‐Protein Interactions with Phage‐Displayed Combinatorial Peptide Libraries
by purification of selected phage by ELISA. Alternatively, there is a bead?based affinity selection method. These methods allow one to readily isolate peptide ligands that bind to a protein target of interest and use the consensus sequence to search proteomic
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