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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Yang QX,Huang FY,Huang TH,Gelbaum Ldoi
10.1016/S0006-3495(93)81486-3subject
Has Abstractpub_date
1993-04-01 00:00:00pages
1361-5issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(93)81486-3journal_volume
64pub_type
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