Title: An unusual red-edge excitation and time-dependent Stokes shift in the single tryptophan mutant protein DD-carboxypeptidase from Streptomyces: The role of dynamics and tryptophan rotamers
Authors: Maglia, Giovanni
Jonckheer, Abel
De Maeyer, Marc
Frere, Jean-Marie
Engelborghs, Yves # ×
Issue Date: Feb-2008
Publisher: Cold spring harbor lab press, publications dept
Series Title: Protein science vol:17 issue:2 pages:352-361
Abstract: The fluorescence emission of the single tryptophan (W233) of the mutant protein DD-carboxypeptidase from streptomyces is characterized by a red-edge excitation shift (REES), i.e., the phenomenon that the wavelength of maximum emission depends on the excitation wavelength. This phenomenon is an indication for a strongly reduced dynamic environment of the single tryptophan, which has a very low accessibility to the solvent. The REES shows, however, an unusual temperature and time dependence. This, together with the fluorescence lifetime analysis, showing three resolvable lifetimes, can be explained by the presence of three rotameric states that can be identified using the Dead-End Elimination method. The three individual lifetimes increase with increasing emission wavelength, indicating the presence of restricted protein dynamics within the rotameric states. This is confirmed by time-resolved anisotropy measurements that show dynamics within the rotamers but not among the rotamers. The global picture is that of a protein with a single buried tryptophan showing strongly restricted dynamics within three distinct rotameric states with different emission spectra and an anisotropic environment.
ISSN: 0961-8368
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry, Molecular and Structural Biology Section
Research Group Neurophysiology
Laboratory for Auditive Neurophysiology
× corresponding author
# (joint) last author

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