Marc-Antoine Sani University of Melbourne
10 protocols

Ashish Sethi
  • Post-Doc, University of Melbourne
Research focus
  • Biophysics
  • Structure Biology, solution NMR, Protein-ligand binding, Protein dynamics


PhD, University of Melbourne, 2017

Lab information


• Bruell S* & Sethi A*, Smith N, Scott D.J, Hossain A, Wu Q.P, Guo Z.Y, Petrie E.J, Gooley P.R, Bathgate R.A.D “Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin” published in Nature Scientific Reports on June 12, 2017. (* Co-first author)
• Sethi A, Bruell S, Patil N, Hossain A, Scott D.J, Petrie E.J, Bathgate R.A.D, Gooley P.R. “The complex binding mode of the peptide hormone H2 relaxin to its receptor RXFP1” published in Nature Communications on April 18, 2016.
• Sethi A, Mohanty B, Ramasubbu N, Gooley P.R “Structure of amylase binding protein A of Streptococcous gordonii: a potential receptor for human salivary α-amylase enzyme” published in Protein Science on April 2, 2015.
• Tailhades J, Sethi A, Petrie E, Gooley P.R. “Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein” published in Chemistry A European Journal on November 27, 2015.
• Petrie E.J, Lagaida S, Sethi A, Bathgate R.A.D, Gooley P.R. “In a class of their own – RXFP1 and RXFP2 are unique members of the LGR family ” published in Frontiers in Endocrinology on September 7, 2015.

1 Protocol reviewed
Nitroxide Labeling of Proteins and the Determination of Paramagnetic Relaxation Derived Distance Restraints for NMR Studies
Authors:  Megan Sjodt and Robert T. Clubb, date: 04/05/2017, view: 2387, Q&A: 0
Site-specific attachment of paramagnetic spin labels to biomolecules causes distance-dependent line-broadening effects, which can be exploited to study the structure and dynamics of these molecules in solution. This protocol describes how to attach ...
More >