ArticleThe journal of physical chemistry letters2014
Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.
Article in The journal of physical chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Accurate Machine Learning Prediction of Protein Circular Dichroism Spectra with Embedded Density Descriptors.JACS Au · 2021Article
- Near-Ultraviolet Circular Dichroism and Two-Dimensional Spectroscopy of Polypeptides.Molecules (Basel, Switzerland) · 2021Article
- Steady-State Linear and Non-linear Optical Spectroscopy of Organic Chromophores and Bio-macromolecules.Frontiers in chemistry · 2018Review
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Authors and funding
4 authors.
Funding
Abstract
The function of protein relies on their folding to assume the proper structure. Probing the structural variations during the folding process is crucial for understanding the underlying mechanism. We present a combined quantum mechanics/molecular dynamics simulation study that demonstrates how coherent resonant nonlinear ultraviolet spectra can be used to follow the fast folding dynamics of a mini-protein, Trp-cage. Two dimensional ultraviolet signals of the backbone transitions carry rich information of both local (secondary) and global (tertiary) structures. The complexity of signals decreases as the conformational entropy decreases in the course of the folding process. We show that the approximate entropy of the signals provides a quantitative marker of protein folding status, accessible by both theoretical calculations and experiments.
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Registered trials
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