ArticleMethods in enzymology2021
Incorporation of proline analogs into recombinant proteins expressed in Escherichia coli.
Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- A Photo-Crosslinked Casein-Tannic Acid System for Enhanced Hair Protection: A Green Chemistry Approach.Polymers · 2025Article
- Site-Specific Incorporation of Fluorinated Prolines into Proteins and Their Impact on Neighbouring Residues.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
- 4-Thiaproline accelerates the slow folding phase of proteins containing cis prolines in the native state by two orders of magnitude.Protein science : a publication of the Protein Society · 2024Article
- Incorporation of Aliphatic Proline Residues into Recombinantly Produced Insulin.ACS chemical biology · 2023Article
- Structural basis of lipid-droplet localization of 17-beta-hydroxysteroid dehydrogenase 13.Nature communications · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Proline residues are unique in the extent to which they constrain the conformational space available to the protein backbone. Because the conformational preferences of proline cannot be recapitulated by any of the other proteinogenic amino acids, standard mutagenesis approaches that seek to introduce new chemical functionality at proline positions unavoidably perturb backbone flexibility. Here, we detail the incorporation of proline analogs into recombinant proteins in Escherichia coli via a residue-specific mutagenesis strategy. This approach results in global replacement of proline residues with high yields of the recombinant protein of interest, minimal genetic manipulation, and maintenance of backbone conformational constraints.
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Registered trials
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