Facility manager: Pál Stráner
Modern gene and biotechnology made possible to expression (e.g. in bacterial systems), (re)design, point mutation, etc. of natural and denovo proteins. By using recombinant DNA techniques we are expressing short, 20-30 amino acid comprising miniproteins, as well as longer multidomain proteins composed of hundreds of residues. The nonselective isotope incorporation (15N and/or, 13C) as well as the residue specific isotope labeling is also possible. Miniproteins are expressed via fusion expression systems, with fusion partner proteins such as Ubiquitin, GFP, etc..
Great success of a small-, (mini)-protein
Expression and non-selective isotope labelling was a precondition of our research project aiming to characterise “invisible” intermediate structures of some Trp-cage miniproteins via temperature dependent NMR (1H-15N-HSQC) measurements.
Pál Stráner , Nóra Taricska , Mária Szabó , Gábor K. Tóth , András Perczel
Bacterial expression and/or solid phase peptide synthesis of 20-40 amino acid long polypeptides and miniproteins, the case study of Class B GPCR ligands
Curr. Prot. Pept. Sci. 17(2):147-155. DOI: 10.2174/1389203716666151102105215 | PMID: 26521952 (2016) Kivonat