Calorimetric and spectroscopic investigation of the interaction between the C-terminal domain of Enzyme I and its ligands

Podobne zapisy

• Thermodynamic dissection of large-scale domain motions coupled with ligand binding of enzyme I
  od: Yun, Young-Joo, i wsp.
  Wydane: (2013)
• Calorimetric and spectroscopic investigation of drug-DNA interactions. I. The binding of netropsin to poly d(AT).
  od: Marky, L A, i wsp.
  Wydane: (1983)
• Impact of Phosphorylation on Structure and Thermodynamics of the Interaction between the N-terminal Domain of Enzyme I and the Histidine Phosphocarrier Protein of the Bacterial Phosphotransferase System
  od: Suh, Jeong-Yong, i wsp.
  Wydane: (2008)
• Calorimetric and spectroscopic investigation of drug--DNA interactions: II. Dipyrandium binding to poly d(AT).
  od: Marky, L A, i wsp.
  Wydane: (1983)
• Dimerization facilitates the conformational transitions for bacterial phosphotransferase enzyme I autophosphorylation in an allosteric manner
  od: Lee, Ko On, i wsp.
  Wydane: (2017)