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- W2010453648 abstract "The mechanism by which the intrinsic fiuorescence of tryptophan residues in α-lytic protease and lysozyme are quenched by a complex formed between the single histidine residue in each protein and Ru(III)(NH3)5 was investigated. The R0 values for α-lytic protease and lysozyme were 15.5 and 11.8 Å, respectively. Good agreement between the efficiency of energy transfer measured experimentally and that calculated from the X-ray data, assuming the Förster dipole-dipole mechanism, demonstrates that this mechanism is appropriate. The ease with which the ruthenium-labeled enzymes can be synthesized and purified suggests that the Ru(III)(NH3)5-His complex may have general utility in structural studies of proteins in solution." @default.
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- W2010453648 date "1982-03-01" @default.
- W2010453648 modified "2023-10-05" @default.
- W2010453648 title "Interresidue distance measurements in proteins Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in α-lytic protease and lysozyme" @default.
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- W2010453648 doi "https://doi.org/10.1016/0167-4838(82)90032-2" @default.
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