The effect of hydration on the dynamics of trimethoprim bound to dihydrofolate reductase. A deuterium NMR study

Q. X. Yang, F. Y. Huang, T. H. Huang, L. Gelbaum

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To determine the effect of hydration on the dynamics of a protein complex, we used deuterium nuclear magnetic resonance (NMR) techniques to examine a trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complex in its lyophilized, partially hydrated, polycrystalline, and ammonium sulfate-precipitated states. The results indicate that TMP is rigid in the lyophilized powder state. The dynamic behavior could be restored by partial rehydration. At 30 wt% hydration the deuterium spectrum of the partially hydrated sample was indistinguishable from that of the polycrystalline and ammonium sulfate-precipitated samples, suggesting that the structure of the protein/TMP complex is similar in the three physical states. Furthermore, we found that the para- and meta-methoxyl groups have very different dynamical behavior.

Original languageEnglish
Pages (from-to)1361-1365
Number of pages5
JournalBiophysical Journal
Issue number4
Publication statusPublished - 1993 Jan 1


ASJC Scopus subject areas

  • Biophysics

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