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Chemical Synthesis of PDZ Domains. | LitMetric

Chemical Synthesis of PDZ Domains.

Methods Mol Biol

Department of Drug Design and Pharmacology, Center for Biopharmaceuticals, University of Copenhagen, Copenhagen, Denmark.

Published: June 2021

AI Article Synopsis

  • Advances in chemical protein synthesis now allow for the creation of custom proteins with various modifications, leading to better control over posttranslational modifications (PTMs).
  • Expressed protein ligation (EPL) is utilized to incorporate specific amino acid analogs and mutations in PDZ (postsynaptic density) protein domains, facilitating the study of their protein-protein interactions (PPIs).
  • The text provides protocols for performing EPL on PDZ domains, specifically highlighting modifications related to phosphorylation and amide-to-ester changes.

Article Abstract

Developments in chemical protein synthesis have enabled the generation of tailor-made proteins including incorporation of many types of modifications into proteins, enhancing our ability to control site-specificity of protein posttranslational modifications (PTMs), modify protein backbones and introduce photocrosslinking probes. For PDZ (postsynaptic density protein, disks large, zonula occludens) protein domains, expressed protein ligation (EPL) has been employed to introduce analogs of cognate amino acids, amide-to-ester bond mutations, and phosphorylations in the study of PDZ domain-mediated protein-protein interactions (PPIs). Here, we present protocols for EPL of PDZ domains focusing on phosphorylation and amide-to-ester modifications in the PDZ domain proteins.

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Source
http://dx.doi.org/10.1007/978-1-0716-1166-1_12DOI Listing

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