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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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Citations
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Journal ArticleDOI

Power-law intermittency of single emitters

TL;DR: In this article, the authors summarize experimental observations of fluorescence intermittency of single semiconductor nanocrystals and single molecules and argue that a self-trapping model with a distribution of trapping distances can account for most, if not all, observations.
Journal ArticleDOI

Principal Component Analysis for Protein Folding Dynamics

TL;DR: The effectiveness of principal components analysis (PCA), an already established mathematical technique for finding global, correlated motions in atomic simulations of proteins, is evaluated here for coarse-grained trajectories.
Journal ArticleDOI

RNA and protein folding: common themes and variations.

TL;DR: The iterative annealing mechanism, introduced to describe chaperonin-mediated folding, can be generalized to understand protein-assisted RNA folding and provides a unified theory of RNA and protein folding.
Journal ArticleDOI

Single-molecule biophysics: at the interface of biology, physics and chemistry

TL;DR: An overview of the burgeoning field of single-molecule biophysics is presented, discussing key highlights and selected examples from its genesis to the authors' projections for its future.
Journal ArticleDOI

Energy flow in proteins.

TL;DR: This work reviews work that addresses connections between globular proteins, percolation clusters, and the similarity of energy flow and thermal transport in these systems and reviews experimental and theoretical studies of the anisotropic flow of energy through the vibrational states of a protein.
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.
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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.
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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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