ArticleProtein expression and purification2009
Expression and purification of isotopically labeled peptide inhibitors and substrates of cAMP-dependant protein kinase A for NMR analysis.
Article in Protein expression and purification, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds.Antibiotics (Basel, Switzerland) · 2020Review
- Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.Cellular signalling · 2014Article
- Inflammatory Regulation Effect and Action Mechanism of Anti-Inflammatory Effective Parts of Housefly (Musca domestica) Larvae on Atherosclerosis.Evidence-based complementary and alternative medicine : eCAM · 2013Article
- cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban.Journal of molecular biology · 2011Article
- Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase.Journal of molecular biology · 2011Article
- Dynamics connect substrate recognition to catalysis in protein kinase A.Nature chemical biology · 2010Article
- One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements.Journal of the American Chemical Society · 2009Article
- High-level expression and large-scale preparation of soluble HBx antigen from Escherichia coli.Biotechnology and applied biochemistry · 2009Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Extensive X-ray crystallographic studies carried out on the catalytic-subunit of protein kinase A (PKA-C) enabled the atomic characterization of inhibitor and/or substrate peptide analogues trapped at its active site. Yet, the structural and dynamic transitions of these peptides from the free to the bound state are missing. These conformational transitions are central to understanding molecular recognition and the enzymatic cycle. NMR spectroscopy allows one to study these phenomena under functionally relevant conditions. However, the amounts of isotopically labeled peptides required for this technique present prohibitive costs for solid-phase peptide synthesis. To enable NMR studies, we have optimized both expression and purification of isotopically enriched substrate/inhibitor peptides using a recombinant fusion protein system. Three of these peptides correspond to the cytoplasmic regions of the wild-type and lethal mutants of the membrane protein phospholamban, while the fourth peptide correspond to the binding epitope of the heat-stable protein kinase inhibitor (PKI(5-24)). The target peptides were fused to the maltose binding protein (MBP), which is further purified using a His(6) tag approach. This convenient protocol allows for the purification of milligram amounts of peptides necessary for NMR analysis.
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