title: Investigating the structural origin of trpzip2 temperature dependent unfolding fluorescence line shape based on a Markov state model simulation.
abstract: Vibrationally resolved fluorescence spectra of the β-hairpin trpzip2 peptide at two temperatures as well as during a T-jump unfolding process are simulated on the basis of a combination of Markov state models and quantum chemistry schemes. The broad asymmetric spectral line shape feature is reproduced by considering the exciton-phonon couplings. The temperature dependent red shift observed in the experiment has been attributed to the state population changes of specific chromophores. Through further theoretical study, it is found that both the environment's electric field and the chromophores' geometry distortions are responsible for tryptophan fluorescence shift.
authors.affiliation: State Key Lab of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Dalian, 116023, China.
authors.forename: Jian
authors.initials: J
authors.lastname: Song
authors.forename: Fang
authors.initials: F
authors.lastname: Gao
authors.forename: Raymond Z
authors.initials: RZ
authors.lastname: Cui
authors.forename: Feng
authors.initials: F
authors.lastname: Shuang
authors.forename: Wanzhen
authors.initials: W
authors.lastname: Liang
authors.forename: Xuhui
authors.initials: X
authors.lastname: Huang
authors.forename: Wei
authors.initials: W
authors.lastname: Zhuang
mesh_terms: D005453:Fluorescence; D008958:Models, Molecular; D011487:Protein Conformation; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013997:Time Factors; D014732:Vibration
chemical_list: D011506:Proteins; C539234:Trpzip2 protein