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
This thesis demonstrates the applicability of room temperature tryptophan phosphorescence to a varie...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
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...
In the present study the distance dependence of tryptophan-disulfide interaction is examined with a ...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The aromatic amino acids, tryptophan and tyrosine exhibited fluorescence and phosphorescence at 77°K...
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphor...
Time-resolved fluorescence study of single tryptophan-containing proteins, nuclease, ribonuclease T1...
AbstractThe fluorescence intensity and anisotropy decays of the intrinsic tryptophan emission from s...
Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single ...
Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single ...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
This thesis demonstrates the applicability of room temperature tryptophan phosphorescence to a varie...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
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...
In the present study the distance dependence of tryptophan-disulfide interaction is examined with a ...
The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand bi...
The aromatic amino acids, tryptophan and tyrosine exhibited fluorescence and phosphorescence at 77°K...
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphor...
Time-resolved fluorescence study of single tryptophan-containing proteins, nuclease, ribonuclease T1...
AbstractThe fluorescence intensity and anisotropy decays of the intrinsic tryptophan emission from s...
Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single ...
Visible fluorescent proteins from Aequorea victoria contain next to the fluorophoric group a single ...
The single room temperature phosphorescent (RTP) residue of horse liver alcohol dehydrogenase (LADH)...
This thesis demonstrates the applicability of room temperature tryptophan phosphorescence to a varie...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...