Hexamerization of the bacteriophage T4 capsid protein gp23 and its W13V mutant studied by time-resolved tryptophan fluorescence

Time-resolved and steady-state fluorescence of the intrinsic protein fluorophore tryptophan is used to study the bacteriophage T4 capsid protein gp23. Denaturation of the N-terminus in hexameric wild type gp23 is observed around 40 degrees C, additionally the lifetimes obtained from time-resolved fluorescence measurements could tentatively be assigned to specific trytophan residues with the help of homology model of gp23.