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Comparison of the Time‐resolved Absorption and Phosphorescence from the Tryptophan Triplet State in Proteins in Solution
Author(s) -
Gershenson Anne,
Gafni Ari,
Steel Duncan
Publication year - 1998
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1998.tb05216.x
Subject(s) - phosphorescence , tryptophan , triplet state , absorption (acoustics) , photochemistry , chemistry , state (computer science) , fluorescence , physics , optics , molecule , biochemistry , organic chemistry , computer science , amino acid , algorithm
Measurement of the room temperature Trp triplet state lifetime in proteins by time‐resolved phosphorescence can provide valuable information on the structure and dynamics of proteins in solution. Our time‐resolved absorption measurements on the long‐lived states resulting from electronic excitation of the chromophore demonstrate the presence of more complex behavior than revealed by time‐resolved phosphorescence. To provide additional insight into this behavior, a comparative study of time‐resolved transient absorption and time‐resolved phosphorescence of proteins in solution was carried out. The results show that the time evolution of the long‐lived states observed through transient absorption often differs considerably from that observed in time‐resolved phosphorescence. In some proteins, the presence of competing reactions complicates the interpretation of the transient absorption measurements (which may affect the phosphorescence yield). A more complete characterization of these processes will likely prove useful in the study of protein structure and dynamics in solution.