The programs for the decomposition of protein tryptophan spectra measured in absence (Single spectrum) and presence (Multiple spectra) of external quenchers of tryptophan fluorescence could be downloaded. The programs are designed for Windows 32-bit platforms and run using Visual Basic platform.

Programs and input files should be stored in C:\VB-6 directory (the path could be changed only by making changes in the code of programs). All output files will be generated to the same directory.

The program for the decomposition of single spectrum and examples of input and output files (see explanation in FCAT module)

Single spectra

The program for the decomposition of multiple spectra measured at various concentrations of external quenchers and examples of input and output files (see explanation in FCAT module)

Multiple spectra

Papers for download

Hixon, J & Y.K.Reshetnyak (2009) Algorithm for the Analysis of Tryptophan Fluorescence Spectra and Their Correlation with Protein Structural Parameters. Algorithms, 2, 1155-1176; doi:10.3390/a2031155

Reshetnyak, Y.K., Segala, M., Andreev, O.A., & Engelman, D.M. (2007) A monomeric membrane peptide that lives in three worlds: in solution, attached to and inserted across lipid bilayers. Biophysical J. 93(7), 2363-72.

C. Shen, R. Menon, D. Das, N. Bansal, N. Nahar, N. Guduru, S. Jaegle, J. Peckham, Y. K. Reshetnyak (2008) The Protein Fluorescence And Structural Toolkit (PFAST): Database and programs for the analysis of protein fluorescence and structural data. Protein: Structure, Function, and Bioinformatics, 71, 1744-1754.

Burstein, E.A., S.M. Abornev, and Y.K. Reshetnyak. 2001 Decomposition of Protein Tryptophan Fluorescence Spectra into Log-Normal Components. I. Decomposition Algorithms, Biophys. J. , 81: 1699-1709.

Reshetnyak, Y.K., and E.A. Burstein. 2001. Decomposition of Protein Tryptophan Fluorescence Spectra into Log-Normal Components. II. The Statistical Proof of Discreteness of Tryptophan Classes in Proteins, Biophys. J ., 81:1710-1734.

Reshetnyak, Y.K. , Y. Koshevnik, and E.A. Burstein. 2001 Decomposition of Protein Tryptophan Fluorescence Spectra into Log-Normal Components. III. Correlation between Fluorescence and Microenvironment Parameters of Individual Tryptophan Residues, Biophys. J ., 81: 1735-1758.

Burstein, E.A., and V.I. Emelyanenko. 1996. Log-normal description of fluorescence spectra of organic fluorophores. Photochem. Photobiol. 64: 316-320.

Burstein, E.A., N.S. Vedenkina, and M.N. Ivkova. 1973. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18: 263-279.

Linke, D., J. Frank, M.S. Pope, J. Soll, I. Ilkavets, P. Fromme, E.A. Burstein, Y.K. Reshetnyak, and V.I. Emelyanenko. 2004. Folding Kinetics and Structure of OEP16, Biophys.J., 86: 1479-1487.

Orlov, N.Ya, T.G. Orlova, Y.K. Reshetnyak, E.A. Burstein, and N. Kimura. 1999. Comparative study of recombinant rat nucleoside diphosphate kinases alpha and beta by intrinsic protein fluorescence, J Biomol Struct Dyn , 16: 955-68.

Reshetnyak YK, Tchedre KT, Nair MP, Pritchard PH, Lacko AG Structural differences between wild-type and fish eye disease mutant of Lecithin:cholesterol acyltransferase , J Biomol Struct Dynamics 2006; 2 4:75-82

Reshetnyak, Ya.K., O.A. Andreev, J. Borejdo, D.D. Toptygin, L. Brand, and E. A. Burstein. 2000. The Identification of Tryptophan Residues Responsible for ATP-induced Increase in Intrinsic Fluorescence of Myosin Subfragment 1, J Biomol. Struct. Dynamics , 18: 113-125.

Reshetnyak, Ya.K., R.P. Kitson, M. Lu, and R.H. Goldfarb. 2004. Conformational and enzymatic changes of 20S proteasome of rat natural killer cells induced by mono and divalent cations. J. Struct. Biol. , 145: 263-271.

Torrent M, Cuyás E, Carreras E, Navarro S, López O, de la Maza A, Nogués M V, Reshetnyak YK, Boix E Topology studies on the membrane interaction mechanism of the eosinophil cationic protein Biochemistry 2007; 46:720-733

Emelyanenko V.I., Y.K. Reshetnyak, O.A. Andreev, and E.A. Burstein. 2000 Log-normal component analysis of fluorescence spectra of Prodan and Acrylodan bound to proteins, Biophysics , 45: 207-219.