@article{4c9f0ddde040462b927302ce207822e8,
title = "The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study",
abstract = "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.",
keywords = "Conformation, Dihydrofolate reductase, E. coli, NMR, N, P, NADP, Trimethoprim",
author = "Huang, {Fu yung} and Yang, {Qing Xian} and Huang, {Tai huang} and Leslie Gelbaum and Kuyper, {Lee F.}",
note = "Funding Information: Acknowledgemems: We wish to thank Dr, E. Howell of University of Tennessc for lh¢ l\]¢rllrotl~g ill of{"} lh~ DHFR over.praducing E, col/ strain. Technical assistancc.,so f M~. L.E. Khaw is ~¢knowlcdlt,¢d, This work is supported by Grant GM-39779 from Natlonal lnstitul¢ of Health.",
year = "1991",
month = may,
day = "20",
doi = "10.1016/0014-5793(91)80549-I",
language = "English",
volume = "283",
pages = "44--46",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",
}