Dielectric relaxation in a single tryptophan protein.
TLDR
A remarkable blue shift in fluorescence upon bimolecular quenching in the single‐tryptophan thermostable protein Bj2S, the 2S seed albumin from Brassica juncea, at ambient temperature and viscosity is reported.About:
This article is published in FEBS Letters.The article was published on 2001-12-07 and is currently open access. It has received 11 citations till now. The article focuses on the topics: Quenching (fluorescence) & Fluorescence.read more
Citations
More filters
Journal ArticleDOI
The interaction of heparin/polyanions with bovine, porcine, and human growth hormone.
TL;DR: In this paper, a thermodynamic description of the interaction of four representative polyanions with human, bovine, and porcine growth hormone is described, and the potential biological significance of growth hormone polyanion interactions is discussed.
Journal ArticleDOI
Time-resolved emission spectra of green fluorescent protein
Andrew A. Jaye,Andrew A. Jaye,Deborah Stoner-Ma,Pavel Matousek,Michael Towrie,Peter J. Tonge,Stephen R. Meech +6 more
TL;DR: In this article, the emission spectra of wild-type green fluorescent protein (wtGFP) and the T203V GFP mutant have been recorded with picosecond time resolution, allowing the separate characterization of the two spectral components associated with the neutral and anionic forms of the GFP chromophore.
Symposium-in-Print: Green Fluorescent Protein and Homologs Time-Resolved Emission Spectra of Green Fluorescent Protein
TL;DR: In this article, the emission spectra of wild-type green fluorescent protein (wtGFP) and the T203V GFP mutant have been recorded with picosecond time resolution, allowing the separate characterization of the two spectral components associated with the neutral and anionic forms of the GFP chromophore.
Journal ArticleDOI
Dissecting Nanosecond Dynamics in Membrane Proteins with Dipolar Relaxation upon Tryptophan Photoexcitation.
TL;DR: The results demonstrate that ultrafast, subnanosecond relaxation reports on the extent of Trp shielding from water, with micelle and protein moieties making additive contributions, thereby probing conformational dynamics around the intrinsic fluorophore.
Journal ArticleDOI
The recovery of dipolar relaxation times from fluorescence decays as a tool to probe local dynamics in single tryptophan proteins.
TL;DR: A new algorithm taking into account the relaxation effect has been applied to the fluorescence decay function obtained by phase-shift and demodulation data, suggesting the presence of a relaxation process even in proteins that lack a lifetime-dependent spectral shift.
References
More filters
Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
Mechanisms of Tryptophan Fluorescence Shifts in Proteins
James T. Vivian,Patrik R. Callis +1 more
TL;DR: This study predicted the fluorescence wavelengths of 19 tryptophans in 16 proteins using a hybrid quantum mechanical-classical molecular dynamics method with the assumption that only electrostatic interactions of thetryptophan ring electron density with the surrounding protein and solvent affect the transition energy.
Journal ArticleDOI
Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies.
TL;DR: The value of this probing technique lies in its ability to sense not only the steady-state exposure of a residue in a protein, but also its dynamic exposure.
Journal ArticleDOI
Dynamics of Solvation and Charge Transfer Reactions in Dipolar Liquids
TL;DR: In this article, the effects of solvent and solvent dynamics on chemical reactions, especially on charge transfer processes, have long been a subject of great importance in physical chemistry, and an understanding of the timedependent response of a polar solvent to a changing charge distribution in a polar solute molecule is essential to understand the role of solvent in many important chemical and biological processes in liquids.
Book
Ultraviolet Spectroscopy of Proteins
TL;DR: The present work presents a meta-analysis of the dynamics of proteins in the presence of a high-temperature environment and investigates the role of derivative Spectroscopy in this phenomenon.