The effect of hydration on the dynamics of trimethoprim bound to dihydrofolate reductase. A deuterium NMR study.
Related Articles The effect of hydration on the dynamics of trimethoprim bound to dihydrofolate reductase. A deuterium NMR study.
Biophys J. 1993 Apr;64(4):1361-5
Authors: Yang QX, Huang FY, Huang TH, Gelbaum L
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.
PMID: 8494990 [PubMed - indexed for MEDLINE]
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PubMed