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Journal ArticleDOI

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

TLDR
By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, the variation of flavin-tyrosine distance over time is observed, suggesting the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.
Abstract
Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe the variation of flavin-tyrosine distance over time. We could then determine the potential of mean force between the flavin and the tyrosine, and a correlation analysis revealed conformational fluctuation at multiple time scales spanning from hundreds of microseconds to seconds. This phenomenon suggests the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.

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Dissertation

From Brownian motion to supercooled water in confinements - a molecular dynamics simulation study

Felix Klameth
TL;DR: In this paper, the authors used power-law waiting time distributions to describe motion in a harmonic potential of water in confinements and found that the surface strongly affects the structure of water.
Journal ArticleDOI

Tracking structural transitions of bovine serum albumin in surfactant solutions by fluorescence correlation spectroscopy and fluorescence lifetime analysis

TL;DR: Fluorescence correlation spectroscopy is employed to track the structural transition of bovine serum albumin in low concentrated cationic, anionic, and nonionic surfactant solutions and identifies whether the structural change of protein results from its self-aggregation or unfolding.
Journal ArticleDOI

Anomalous lineshapes and aging effects in two-dimensional correlation spectroscopy

TL;DR: The signatures of anomalous relaxation in two-dimensional four wave mixing signals are analyzed using the continuous time random walk model for spectral diffusion to analyze their optical response to sequences of ultrashort optical pulse.
Journal ArticleDOI

Stretching of single poly-ubiquitin molecules revisited: dynamic disorder in the non-exponential unfolding kinetics.

TL;DR: This work suggests a sound and plausible alternative interpretation for the non-exponential kinetics in the stretching of poly-ubiquitin molecules, associated with dynamic disorder.
References
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疟原虫var基因转换速率变化导致抗原变异[英]/Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A

宁北芳, +1 more
TL;DR: PfPMP1)与感染红细胞、树突状组胞以及胎盘的单个或多个受体作用,在黏附及免疫逃避中起关键的作�ly.
Journal ArticleDOI

Electron transfers in chemistry and biology

TL;DR: In this paper, the electron transfer reactions between ions and molecules in solution have been the subject of considerable experimental study during the past three decades, including charge transfer, photoelectric emission spectra, chemiluminescent electron transfer, and electron transfer through frozen media.
Journal ArticleDOI

Formation of glasses from liquids and biopolymers.

TL;DR: The onset of a sharp change in ddT( is the Debye-Waller factor and T is temperature) in proteins, which is controversially indentified with the glass transition in liquids, is shown to be general for glass formers and observable in computer simulations of strong and fragile ionic liquids, where it proves to be close to the experimental glass transition temperature.
Journal ArticleDOI

The energy landscapes and motions of proteins.

TL;DR: The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
Journal ArticleDOI

Fluorescence spectroscopy of single biomolecules.

TL;DR: The progress in applying single-molecule detection and single-Molecule spectroscopy at room temperature by laser-induced fluorescence with the use of fluorophores that are site-specifically attached to macromolecules is reviewed.
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