ArticleProtein science : a publication of the Protein Society2003
High-yield expression of isotopically labeled peptides for use in NMR studies.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Towards Reverse Vaccinology for Bovine TB: High Throughput Expression of Full Length RecombinantFrontiers in molecular biosciences · 2022Article
- Effects of the lung surfactant protein B construct Mini-B on lipid bilayer order and topography.European biophysics journal : EBJ · 2012Article
- Design of high-affinity S100-target hybrid proteins.Protein science : a publication of the Protein Society · 2009Article
- Preparation of recombinant peptides with site- and degree-specific lysine (13)C-methylation.Biochemistry · 2009Article
- Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR.Protein science : a publication of the Protein Society · 2007Article
- Bcl-XL as a fusion protein for the high-level expression of membrane-associated proteins.Protein science : a publication of the Protein Society · 2005Article
- Using lanthanide ions to align troponin complexes in solution: order of lanthanide occupancy in cardiac troponin C.Protein science : a publication of the Protein Society · 2004Article
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Authors and funding
4 authors.
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Abstract
Fusion protein constructs of the 56 amino acid globular protein GB-1 with various peptide sequences, coupled with the incorporation of a histidine tag for affinity purification, have generated high-yield fusion protein constructs. Methionine residues were inserted into the constructs to generate pure peptides following CNBr cleavage, yielding a system that is efficient and cost effective for isotopic labeling of peptides for NMR studies and other disciplines such as mass spectroscopy. Six peptides of varying sequences and hydrophobicities were expressed using this GB-1 fusion protein technique and produced soluble fusion protein constructs in all cases. The ability to easily express and purify recombinant peptides in high yields is applicable for biomedical research and has medicinal and pharmaceutical applications.
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