ArticleProtein science : a publication of the Protein Society2008
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.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.Journal of the Royal Society, Interface · 2023Article
- Rotamer Dynamics: Analysis of Rotamers in Molecular Dynamics Simulations of Proteins.Biophysical journal · 2019Review
- Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.The journal of physical chemistry. B · 2014Article
- Localization and environment of tryptophans in different structural states of concanavalin A.Journal of fluorescence · 2011Article
- Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stability.Journal of pharmaceutical sciences · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
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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.
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