Amino Acid Fluorescence EEM Data

Fluorescence excitation-emission matrix (EEM) measurements of five laboratory mixtures of tryptophan, tyrosine, and phenylalanine dissolved in phosphate-buffered water. Andersson's thesis specifies pH 7.0. The dataset is a compact benchmark for PARAFAC and other multi-way decomposition methods. The samples were measured on a PE LS50B spectrofluorometer with an excitation slit width of 2.5 nm, an emission slit width of 10 nm, and a scan speed of 1500 nm/s. Each amino acid is expected to contribute approximately one rank-one fluorescence component, making the data a simple benchmark for three-component PARAFAC models. The curated file includes the fluorescence tensor X arranged as sample x emission x excitation (5 x 201 x 61), the concentration matrix Y (5 x 3), emission axis EmAx (250-450 nm), excitation axis ExAx (240-300 nm), DimX, analyte labels, and sample labels. The original source README reports excitation 250-300 nm and an array size of 5 x 51 x 201; this curated release follows the axes and dimensions contained in the distributed MATLAB data file. Original ERDA source package: https://sid.erda.dk/share_redirect/AWqL5T6JCZ. Additional UCPH Chemometrics Research page with figures and PARAFAC discussion: https://ucphchemometrics.com/2023/05/04/amino-acids-fluorescence-data/. Recommended citations are Bro (1998) and Andersson (2000).