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

✍ Scribed by Yang, Q.X.; Huang, F.Y.; Huang, T.H.; Gelbaum, L.


Book ID
119410162
Publisher
Biophysical Society
Year
1993
Tongue
English
Weight
504 KB
Volume
64
Category
Article
ISSN
0006-3495

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We have employed deuterium NMR techniques to determine the dynamics of trimethoprim (TMP) in a binary complex with dihydrofolate reductase (DHFR) or in a ternary complex with DHFR and cofactor NADP+ in the fully hydrated state. TMP was deuterated at the following positions: (2',6'-D2)TMP, (3'-Ome-D3

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## Abstract A detailed study on the deuterium NMR of hydrated collagen in the presence of alkali and alkaline earth salt is reported. The effect of different salts in reducing the deuteron quadrupole splitting are similer at low molar content of salt. At higher salt contents, larger ions are more e