Work

Comparison of the Time‐resolved Absorption and Phosphorescence from the Tryptophan Triplet State in Proteins in Solution

Year: 1998

Type: article

Abstract: 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.

Source: Photochemistry and Photobiology

DOI: 10.1111/j.1751-1097.1998.tb05216.x

Authors: Anne Gershenson, Ari Gafni, Duncan Steel

Institutions: California Institute of Technology, University of Michigan

Language: English

Topic: Photochemistry and Electron Transfer Studies

Subfield: Physical and Theoretical Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute on Aging, National Institute of General Medical Sciences

Awards: G1925028792, G382195731, Michigan Molecular Biophysics Training Program, LASER SPECTROSCOPY OF TRIPLET STATES IN PROTEINS