Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study.
Hoeltzli SD, Frieden C.
Hoeltzli SD, et al. Among authors: frieden c.
Biochemistry. 1998 Jan 6;37(1):387-98. doi: 10.1021/bi971962u.
Biochemistry. 1998.
PMID: 9425060
Using site-directed mutagenesis, these resonances have been assigned to individual tryptophans [Hoeltzli, S. D., and Frieden, C. (1994) Biochemistry 33, 5502-5509], allowing both the native and unfolded environments of each tryptophan to be monitored during the refo …
Using site-directed mutagenesis, these resonances have been assigned to individual tryptophans [Hoeltzli, S. D., and Frieden, C …