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The binding of trimethoprim to bacterial dihydrofolate reductase

✍ Scribed by D.J. Baker; C.R. Beddell; J.N. Champness; P.J. Goodford; F.E.A. Norrington; D.R. Smith; D.K. Stammers

Book ID: 115912723
Publisher: Elsevier Science
Year: 1981
Tongue: English
Weight: 336 KB
Volume: 126
Category: Article
ISSN: 0014-5793
DOI: 10.1016/0014-5793(81)81030-7

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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