A chemometric analysis of ligand-induced changes in intrinsic fluorescence of folate binding protein indicates a link between altered conformational structure and physico-chemical characteristics

Applied Spectroscopy

Volumn 63, Issue 12, 2009, Pages 1315-1322

  Bruun, Susanne W ^a   Holm, J A N ^b   Hansen, Steen Ingemann ^b   Andersen, Charlotte M ^a   Norgaard, Lars ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b HILLERØD HOSPITAL   (Denmark)

Author keywords

Autofluorescence; Changes in protein structure and hydrophobicity; Eem; Excitation emission matrix; Folate binding protein; Ligand binding; Methotrexate; Parafac; Parallel factor analysis; Tryptophan residues

Indexed keywords

AMINO ACIDS; BINS; CONFORMATIONS; FACTOR ANALYSIS; FLUORESCENCE; HYDROPHOBICITY; LIGANDS; MULTIVARIANT ANALYSIS; PROTEINS; SOLVENTS;

AUTOFLUORESCENCE; EXCITATION EMISSION MATRICES; FOLATE-BINDING PROTEIN; LIGAND BINDING; METHOTREXATE; PARAFAC; PARALLEL FACTOR ANALYSIS; PROTEIN STRUCTURES; TRYPTOPHAN RESIDUES;

CHEMICAL ANALYSIS;

EID: 75749136108     PISSN: 00037028     EISSN: None     Source Type: Journal    
DOI: 10.1366/000370209790109076     Document Type: Article

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