Thread: NMR paper The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N an
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Default The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N an
The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N and 31P NMR study.

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

FEBS Lett. 1991 May 20;283(1):44-6

Authors: Huang FY, Yang QX, Huang TH, Gelbaum L, Kuyper LF

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.

PMID: 2037072 [PubMed - indexed for MEDLINE]



Source: PubMed
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