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Molekuliarnaia Biologiia|July 1, 1983
[Polarization of intrinsic fluorescence of proteins. III. Intramolecular submobility of tryptophan residues]I M Kuznetsova, K K TuroverovBiophysical Chemistry|December 31, 1986
What causes the depolarization of trypsin and trypsinogen fluorescence. Intramolecular mobility or non-radiative energy transfer?K K Turoverov, I M KuznetsovaMolekuliarnaia Biologiia|September 1, 1985
[Polarization of intrinsic fluorescence of proteins. IV. Changes in the degree of polarization from the emission spectra]K K Turoverov, I M KuznetsovaMolekuliarnaia Biologiia|May 1, 1983
[Polarization of intrinsic fluorescence of proteins. II. Application for the study of equilibrium dynamics of tryptophan residues]K K Turoverov, I M KuznetsovaBioorganicheskaia Khimiia|March 18, 1999
[Intrinsic fluorescence of globular actin. Features of localization of tryptophan residues]K K Turoverov, I M KuznetsovaTsitologiia|November 20, 1998
[What determines the characteristics of the intrinsic UV-fluorescence of proteins? Analysis of the properties of the microenvironment and features of the localization of their tryptophan residues]I M Kuznetsova, K K TuroverovTsitologiia|November 20, 1998
[Intrinsic UV-fluorescence of proteins as a tool for studying their dynamics]K K Turoverov, I M KuznetsovaBiophysical Chemistry|August 1, 1986
What causes the variation of polarization degree across the emission spectrum of proteins?K K Turoverov, I M KuznetsovaTsitologiia|May 19, 2006
[Structural dynamics, stability and folding of proteins]I M Kuznetsova, V Forge, K K TuroverovBioorganicheskaia Khimiia|March 18, 1999
[Features of the structural organization of inactivated actin--an intermediate form of the protein during the folding-unfolding process]I M Kuznetsova, S Iu Khaĭtlina, K K TuroverovPageof 6