Single-site mutations in a hyperthermophilic variant of the B1 domain of protein G result in self-assembled oligomers.

Abstract excerpt

We have characterized two homologous, single-point core mutants of a 57-residue, hyperthermophilic variant of the B1 domain of protein G (HTB1). These single-point mutations in HTB1 replace a Phe residue in the hydrophobic core with either a Glu or Asp residue. Both of these homologous core-variant mutants undergo significant structural rearrangement from the native, monomeric fold and exist as stable soluble...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Benzothiazoles
• Share to Chromatography, Gel
• Share to Congo Red