Search results for "Protein Engineering"

Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation

2014

Abstract Staphylococcus aureus sortase A is a transpeptidase that is extensively used in various protein research applications. Sortase A is highly selective and does not require any cofactors for the catalysis of protein ligation and, importantly, can be produced in high yields. However, the primary disadvantage of this transpeptidase is its inability to access the recognition site within the highly structured regions of folded substrates. To overcome this problem, we developed an Escherichia coli expression system that produces milligram quantities of circularly closed sortase A; efficient enzyme cyclization was achieved by Synechocystis sp. PCC6803 intein-mediated post-translational spli…

Complexes of carbon nanotubes with ions and macromolecules : studies on electronic conduction properties

2014

Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli

2019

Tyrosine nitration is a post-translational protein modification relevant to various pathophysiological processes. Chemical nitration procedures have been used to generate and study nitrated proteins, but these methods regularly lead to modifications at other amino acid residues. A novel strategy employs a genetic code modification that allows incorporation of 3-nitrotyrosine (3-NT) during ribosomal protein synthesis to generate a recombinant protein with defined 3-NT-sites, in the absence of other post-translational modifications. This approach was applied to study the generation and stability of the 3-NT moiety in recombinant proteins produced in E.coli. Nitrated alpha-synuclein (ASYN) was…

Internalization of novel non-viral vector TAT-streptavidin into human cells

2007

BMC Biotechnology, 7 (1)