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Vibrationally resolved fluorescence spectra of the β-hairpintrpzip2 peptide at two temperatures as well as during a T-jump unfolding process are simulated on the basis of a combinationof Markov state models and quantum chemistry schemes. The broad asymmetricspectral line shape feature is reproduced by considering the exciton–phononcouplings. The temperature dependent red shift observed in the experimenthas been attributed to the state population changes of specific chromophores.Through further theoretical study, it is found that both the environment'selectric field and the chromophores’ geometry distortions areresponsible for tryptophan fluorescence shift. [ABSTRACT FROM AUTHOR]