Titlebook: Enzyme-Mediated Ligation Methods; Timo Nuijens,Marcel Schmidt Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019

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In Vitro and , Cyclization of Target Peptides Using an Asparaginyl Endopeptidase from ,ty or potential oral bioavailability. However, there are few tools available for carrying out this modification. Asparaginyl endopeptidases (AEPs) are a class of enzymes that typically work as proteases, but a subset is highly efficient at cyclization of the peptide backbone. In this chapter we desc

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甜得發(fā)膩

Oafishness

BioID as a Tool for Protein-Proximity Labeling in Living Cells,romiscuous biotin ligase, called BioID, fused to a protein of interest that when expressed in cells can be induced to biotinylate interacting and proximate proteins over a period of hours, thus generating a history of protein associations. These biotinylated proteins are subsequently purified and id

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rheumatology

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,Reprisals in Ireland, 1919–1921,ecursor peptide are coexpressed in the leaves of the model plant ., and cyclization of the target peptide occurs .. Using the in vitro method, purified recombinant OaAEP1. produced in bacteria is used to cyclize the target precursor peptide in vitro.