Energy transfer between excited triplet states of aromatic amino acid residues was observed at 1.4 degrees K. The distance necessary for energy transfer between monomeric tyrosine and tryptophan residues was determined to be roughly 63 A. Total phosphorescence decay rate constants for several proteins were determined while emission corresponding to tyrosine and tryptophan residues was monitored. The observed decay rate constants are interpreted in terms of intramolecular interactions of the polypeptide residues
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphor...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...
Energy transfer between excited triplet states of aromatic amino acid residues was observed at 1.4 d...
The first objective of our research was to accurately measure the phosphorescence lifetime of aqueou...
The first objective of our research was to accurately measure the phosphorescence lifetime of aqueou...
The aromatic amino acids, tryptophan and tyrosine exhibited fluorescence and phosphorescence at 77°K...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
The fluorescence and phosphorescence spectra of model indole compounds and of cod parvalbumin III, a...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
In the present study the distance dependence of tryptophan-disulfide interaction is examined with a ...
Tryptophan phosphorescence decay rates had been used to observe protein dynamics inglucokinase (GK) ...
This thesis demonstrates the applicability of room temperature tryptophan phosphorescence to a varie...
AbstractTyrosine is known to quench the phosphorescence of free tryptophan derivatives in solution, ...
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphor...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...
Energy transfer between excited triplet states of aromatic amino acid residues was observed at 1.4 d...
The first objective of our research was to accurately measure the phosphorescence lifetime of aqueou...
The first objective of our research was to accurately measure the phosphorescence lifetime of aqueou...
The aromatic amino acids, tryptophan and tyrosine exhibited fluorescence and phosphorescence at 77°K...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
The fluorescence and phosphorescence spectra of model indole compounds and of cod parvalbumin III, a...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
In the present study the distance dependence of tryptophan-disulfide interaction is examined with a ...
Tryptophan phosphorescence decay rates had been used to observe protein dynamics inglucokinase (GK) ...
This thesis demonstrates the applicability of room temperature tryptophan phosphorescence to a varie...
AbstractTyrosine is known to quench the phosphorescence of free tryptophan derivatives in solution, ...
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphor...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...
Two-step excitation of retinal in bacteriorhodopsin by visible light is followed by an energy transf...