The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study

Fu yung Huang, Qing Xian Yang, Tai huang Huang*, Leslie Gelbaum, Lee F. Kuyper

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.

Original languageEnglish
Pages (from-to)44-46
Number of pages3
JournalFEBS Letters
Issue number1
Publication statusPublished - 1991 May 20


  • Conformation
  • Dihydrofolate reductase
  • E. coli
  • NMR, N, P, NADP
  • Trimethoprim

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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