NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment.
Here, we report the high yield expression and preliminary structural analysis via solution hetero-nuclear NMR spectroscopy of the recombinant Met-1 human Angiogenin. The analysis reveals a well folded as well as, a monomeric polypeptide. Τhe sequence-specific assignment of its (1)H, (15)N and (13)C resonances at high percentage was obtained. Also, using TALOS+ its secondary structure elements were determined.
Department of Pharmacy, University of Patras, 26504, Patras, Greece.
Aikaterini C
AC
Tsika
Department of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500, Larissa, Greece.
Demetra S M
DS
Chatzileontiadou
Department of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500, Larissa, Greece. ddleonidas@bio.uth.gr.
Demetres D
DD
Leonidas
Department of Pharmacy, University of Patras, 26504, Patras, Greece. G.A.Spyroulias@upatras.gr.
Georgios A
GA
Spyroulias
D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*
C046366:angiogenin; D012259:Ribonuclease, Pancreatic
Angiogenesis; Angiogenin; NMR spectroscopy; RNase superfamily; Recombinant protein expression