Abstract:
:The binding of folate to Lactobacillus casei dihydrofolate reductase in the presence and absence of NADP+ has been studied by 15N NMR, using [5-15N]folate. In the presence of NADP+, three separate signals were observed for the single 15N atom, in agreement with our earlier evidence from 1H and 13C NMR for multiple conformations of this complex [(1982) Biochemistry 21, 5831-5838]. The 15N spectra of the binary enzyme-folate complex provide evidence for the first time that this complex also exists in at least two conformational states. This is confirmed by the observation of two separate resonances for the 7-proton of bound folate, located by two-dimensional exchange spectroscopy.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Birdsall B,De Graw J,Feeney J,Hammond S,Searle MS,Roberts GC,Colwell WT,Crase Jdoi
10.1016/0014-5793(87)81252-8subject
Has Abstractpub_date
1987-06-08 00:00:00pages
106-10issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(87)81252-8journal_volume
217pub_type
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