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The amino acid tryptophan displays emission solvatochromism, an emission maximum that shifts with solvent polarity, which is often used in protein studies to indicate local environment hydrophobicity. Use of tryptophan solvatochromism in time-resolved protein studies has traditionally been complicated due to the undescribed photokinetics that result in a characteristic multiexponential emission decay. For the first time, by application of the photokinetic matrix decomposition (PMD) multivariate curve resolution method to time-resolved emission decay (TRED) data, a distinguishment between ground state heterogeneous (GSH) and excited state reaction (ESR) type photokinetics of tryptophan in solution is made possible. It is found that molecular tryptophan displays two emission spectra that decay independently, suggesting GSH type photokinetics, one at 347 nm with a lifetime of 0.5 ns and one at 363 nm with a lifetime of 3.1 ns. When tryptophan is incorporated into a peptide, mastoparan X, the data similarly contain two emission spectra that decay independently, but are shifted in wavelength. Photobleaching experiments confirm that the PMD method is sensitive to tryptophan emission quenching, and therefore may be applied to determine the photokinetics of tryptophan that occur in proteins. Future applications of PMD analysis of tryptophan TRED data as a bioanalytical tool for further characterizing dynamic protein processes are discussed.