Fluorescence of Lysozyme: Emissions from Tryptophan Residues 62 and 108 and Energy Migration
Taiji Imoto(University of Arizona), Leslie S. Forster(University of Arizona), J.A. Rupley(University of Arizona), Fumio Tanaka(University of Arizona)
Cited by 292Open Access
Abstract
The bulk of the fluorescence of lysozyme is located in Trp 62 and Trp 108. By examination of the fluorescence of derivatives in which Trp 62 and/or Trp 108 are specifically oxidized, it has been possible to detect a pH-dependent interaction between tryptophan residues. This interaction is interpreted as energy transfer from Trp 108 to Trp 62.
Related Papers
Crystallographic studies of the activity of hen egg-white lysozyme
C. C. F. Blake, L.N. Johnson, G. A. Mair et al.|Proceedings of the Royal Society of London. Series B, Biological sciences|1967|653
On the conformation of the hen egg-white lysozyme molecule
C. C. F. Blake, G. A. Mair, A.C.T. North et al.|Proceedings of the Royal Society of London. Series B, Biological sciences|1967|430