Understanding the contribution of individual tryptophan residues to intrinsic lysozyme fluorescence

Title:Understanding the contribution of individual tryptophan residues to intrinsic lysozyme fluorescence

Volume: 7 Issue: 6

Author(s): Irina M. Kuznetsova, Alexander G. Biktashev, Lubov' N. Malova, Natalia A. Bushmarina, Vladimir N. Uversky*Konstantin K. Turoverov

Affiliation:

• lnstitute for Biological Instrumentation, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia
• Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

Abstract: Packing density and other properties of the microenvironment of tryptophan residues in hen egg-white lysozyme macromolecule have been studied on the basis of the known 3D structure of this protein. Results presented here suggest that the efficiency of action of the group which, in principal, can affect tryptophan fluor<;scence depends not only on the distance between this group and the indole ring, but to a great extent upon the location of this group relative to the indole ring.

Cite this article as:

Kuznetsova M. Irina, Biktashev G. Alexander, Malova N. Lubov', Bushmarina A. Natalia, Uversky N. Vladimir*, Turoverov K. Konstantin, Understanding the contribution of individual tryptophan residues to intrinsic lysozyme fluorescence, Protein & Peptide Letters 2000; 7 (6) . https://dx.doi.org/10.2174/092986650706221208100119