Abstract
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 language | English |
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Pages (from-to) | 1361-1365 |
Number of pages | 5 |
Journal | Biophysical Journal |
Volume | 64 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1993 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics