19F-n.m.r. studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofolate reductase. Molecular motion and coenzyme-induced conformational changes.

Benzer Materyaller

• A 1H n.m.r. study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase.
  Yazar:: Antonjuk, D. J., ve diğerleri
  Baskı/Yayın Bilgisi: (1984)
• 3H-n.m.r. studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase.
  Yazar:: Curtis, N, ve diğerleri
  Baskı/Yayın Bilgisi: (1994)
• 31P and 1H n.m.r. studies of coenzyme binding to dihydrofolate reductase [proceedings].
  Yazar:: Birdsall, B, ve diğerleri
  Baskı/Yayın Bilgisi: (1977)
• Proceedings: NMR studies of the binding of substrate analogues to L. casei dihydrofolate reductase.
  Yazar:: Burgen, A S, ve diğerleri
  Baskı/Yayın Bilgisi: (1974)
• Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate.
  Yazar:: Polshakov, V. I., ve diğerleri
  Baskı/Yayın Bilgisi: (1999)