The phototransformation of phytochrome probed by 360 MHz proton NMR spectra
The 360 MHz proton NMR spectra of the Pr and Pfr forms of phytochrome have been recorded to probe the nature of the phytochrome phototransformation (Pr → Pfr). The NMR spectra of aliphatic protons in Pr and Pfr proteins are similar, suggesting that the conformation of both proteins are not drastically different. However, the NMR spectrum of aromatic and the -NH- proton resonance region of Pfr differs significantly from that of Pr, including the absence of a resonance at 6.15 ppm in the former. Differences in the NMR spectra of small and large mol wt phytochromes have also been noted. © 1982 Academic Press, Inc.
Publication Source (Journal or Book title)
Biochemical and Biophysical Research Communications
Song, P., Sarkar, H., Tabba, H., & Smith, K. (1982). The phototransformation of phytochrome probed by 360 MHz proton NMR spectra. Biochemical and Biophysical Research Communications, 105 (1), 279-287. https://doi.org/10.1016/S0006-291X(82)80042-9