Unknown

Dataset Information

0

Time resolved photoelectron spectroscopy of thioflavin T photoisomerization: a simulation study.


ABSTRACT: The excited state isomerization of thioflavin T (ThT) is responsible for the quenching of its fluorescence in a nonrestricted environment. The fluorescence quantum yield increases substantially upon binding to amyloid fibers. Simulations reveal that the variation of the twisting angle between benzothiazole and benzene groups (?1) is responsible for the subpicosecond fluorescence quenching. The evolution of the twisting process can be directly probed by photoelectron emission with energies ? ? 1.0 eV before the molecule reaches the ?1-twisted configuration (~300 fs).

SUBMITTER: Ren H 

PROVIDER: S-EPMC3723713 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Time resolved photoelectron spectroscopy of thioflavin T photoisomerization: a simulation study.

Ren Hao H   Fingerhut Benjamin P BP   Mukamel Shaul S  

The journal of physical chemistry. A 20130429 29


The excited state isomerization of thioflavin T (ThT) is responsible for the quenching of its fluorescence in a nonrestricted environment. The fluorescence quantum yield increases substantially upon binding to amyloid fibers. Simulations reveal that the variation of the twisting angle between benzothiazole and benzene groups (φ1) is responsible for the subpicosecond fluorescence quenching. The evolution of the twisting process can be directly probed by photoelectron emission with energies ε ≥ 1.  ...[more]

Similar Datasets

| S-EPMC7304896 | biostudies-literature
| S-EPMC8404190 | biostudies-literature
| S-EPMC6051996 | biostudies-literature
| S-EPMC4216198 | biostudies-literature
| S-EPMC6082858 | biostudies-other
| S-EPMC7613649 | biostudies-literature
| S-EPMC4401660 | biostudies-literature
| S-EPMC7048418 | biostudies-literature
| S-EPMC4620530 | biostudies-literature
| S-EPMC10895665 | biostudies-literature