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Biophys J, September 2001, p. 1735-1758, Vol. 81, No. 3
and
*Institute of Theoretical and Experimental Biophysics, Russia
Academy of Sciences, Pushchino, Moscow Region, Russia 142290; and
MCI WorldCom, Inc., Richardson, Texas 75081 USA
In our previous paper (Reshetnyak, Ya. K., and E. A. Burstein. 2001. Biophys. J. 81:1710-1734) we
confirmed the existence of five statistically discrete classes of
emitting tryptophan fluorophores in proteins. The differences in
fluorescence properties of tryptophan residues of these five classes
reflect differences in interactions of excited states of tryptophan
fluorophores with their microenvironment in proteins. Here we present a
system of describing physical and structural parameters of
microenvironments of tryptophan residues based on analysis of atomic
crystal structures of proteins. The application of multidimensional
statistical methods of cluster and discriminant analyses for the set of
microenvironment parameters of 137 tryptophan residues of 48 proteins
with known three-dimensional structures allowed us to 1) demonstrate
the discrete nature of ensembles of structural parameters of tryptophan residues in proteins; 2) assign spectral components obtained after decomposition of tryptophan fluorescence spectra to individual tryptophan residues; 3) find a correlation between spectroscopic and
physico-structural features of the microenvironment; and 4) reveal
differences in structural and physical parameters of the microenvironment of tryptophan residues belonging to various spectral classes.
Biophys J, September 2001, p. 1735-1758, Vol. 81, No. 3
© 2001 by the Biophysical Society 0006-3495/01/09/1735/24 $2.00
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