Downloads
The programs for the decomposition of protein tryptophan spectra measured in absence (PKM program) and presence (PKK program)
of external quenchers of tryptophan fluorescence could be downloaded. The programs are designed for Windows 32-bit platforms:
- FCAT: Fluorescence & Correlation Analysis Tool
- Single spectra (PKM)
- Multiple spectra (PKK)
Papers for download
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.