• Corpus ID: 31277735

Great Britain 9 Fn . m . r . studies of 3 ' , 5 '-difluoromethotrexate binding to Latobacillus casei dihydrofolate reductase Molecular motion and coenzyme-induced confonmational changes

@inproceedings{Clore2005GreatB9,
  title={Great Britain 9 Fn . m . r . studies of 3 ' , 5 '-difluoromethotrexate binding to Latobacillus casei dihydrofolate reductase Molecular motion and coenzyme-induced confonmational changes},
  author={G. Marius Clore and Angela M. Gronenborn and Berry Birdsall and James Feeney and Gordon C. K. Roberts},
  year={2005}
}
19F-n.m.r. spectroscopy was used to study the binding of 3',5'-difluoromethotrexate to dihydrofolate reductase (tetrahydrofolate dehydrogenase) from Lactobacillus casei. The benzoyl ring of the bound difluoromethotrexate was found to 'flip' about its symmetry axis, and the rate (7.3 x 10s3-1 at 298 K) and activation parameters for this process were determined by lineshape analysis ofthe 19F-n.m.r. spectrum at a series of temperatures in the range 273-308K. The contributions to the barrier for… 

Figures and Tables from this paper