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Open AccessJournal ArticleDOI

Dielectric relaxation in a single tryptophan protein.

Manasi Ghose, +4 more
- 07 Dec 2001 - 
- Vol. 509, Iss: 2, pp 337-340
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.
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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.

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Citations
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Journal ArticleDOI

Red-edge anisotropy microscopy enables dynamic imaging of homo-FRET between green fluorescent proteins in cells

TL;DR: This methodology represents a novel approach for the dynamic measurement of homo-FRET in live cells that will be of utility in the biological sciences to detect oligomerization and concentration dependent interactions between identically labeled molecules.
Book ChapterDOI

Novel insights into protein structure and dynamics utilizing the red edge excitation shift approach

TL;DR: Red edge excitation shift (REES) as discussed by the authors is a phenomenon that occurs when the solvent shell around a polar fluorophore relaxes and shifts toward the red edge of the absorption band.
Journal ArticleDOI

Precursor of the Inactive 2S Seed Storage Protein from the Indian Mustard Brassica juncea Is a Novel Trypsin Inhibitor CHARACTERIZATION, POST-TRANSLATIONAL PROCESSING STUDIES, AND TRANSGENIC EXPRESSION TO DEVELOP INSECT-RESISTANT PLANTS

TL;DR: A novel trypsin inhibitor from Indian mustard Brassica juncea that is unique in being the precursor of a 2S seed storage protein that can be used in transforming seed crops for protection to their vegetative parts and early seed stages, when insect damage is maximal.
Journal ArticleDOI

The Gas-Phase Absorption Spectrum of a Neutral GFP Model Chromophore

TL;DR: There is strong experimental evidence that, in terms of absorption, the conditions in the hydrophobic interior of this protein are very close to those in vacuum, and the absorption of GFP is primarily determined by intrinsic chromophore properties.
Journal ArticleDOI

Napin from Brassica juncea: Thermodynamic and structural analysis of stability

TL;DR: In silico alignment of sequences of napin has revealed that the internal repeats spanning residues 31 to 60 and 73 to 109 are conserved in all Brassica species, which may contribute to the greater stability of nap in nature.
References
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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

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.
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