Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function

Míreanna Comhchosúla

• Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.
  le: Yang, Y R, et al.
  Foilsithe: (1993)
• Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase.
  le: Graf, R, et al.
  Foilsithe: (1996)
• In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains
  le: Ni, Xinhai, et al.
  Foilsithe: (2001)
• In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
  le: Zhang, P., et al.
  Foilsithe: (1996)
• In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.
  le: Yang, Y. R., et al.
  Foilsithe: (1993)