Ontology highlight
ABSTRACT:
SUBMITTER: Osborne MJ
PROVIDER: S-EPMC2366930 | biostudies-literature | 2003 Oct
REPOSITORIES: biostudies-literature
Osborne Michael J MJ Venkitakrishnan Rani P RP Dyson H Jane HJ Wright Peter E PE
Protein science : a publication of the Protein Society 20031001 10
Heteronuclear NMR methods have been used to probe the conformation of four complexes of Escherichia coli dihydrofolate reductase (DHFR) in solution. (1)H(N), (15)N, and (13)C(alpha) resonance assignments have been made for the ternary complex with folate and oxidized NADP(+) cofactor and the ternary complex with folate and a reduced cofactor analog, 5,6-dihydroNADPH. The backbone chemical shifts have been compared with those of the binary complex of DHFR with the substrate analog folate and the ...[more]