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Jingyi Fei

Researcher at University of Chicago

Publications -  66
Citations -  2863

Jingyi Fei is an academic researcher from University of Chicago. The author has contributed to research in topics: RNA & Transfer RNA. The author has an hindex of 24, co-authored 59 publications receiving 2289 citations. Previous affiliations of Jingyi Fei include Columbia University & University of Science and Technology of China.

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Learning Rates and States from Biophysical Time Series: A Bayesian Approach to Model Selection and Single-Molecule FRET Data

TL;DR: It is demonstrated how model selection in such probabilistic or generative modeling can facilitate analysis of closely related temporal data currently prevalent in biophysics, and how this technique can be applied to temporal data such as smFRET time series.
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Coupling of Ribosomal L1 Stalk and tRNA Dynamics during Translation Elongation

TL;DR: It is found that an interaction between the ribosomal L1 stalk and the newly deacylated tRNA is established spontaneously upon peptide bond formation, and it is demonstrated that binding of EF-G shifts the equilibrium toward the ratcheted state.
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Real-time observation of DNA recognition and rejection by the RNA-guided endonuclease Cas9.

TL;DR: Single-molecule FRET is used to probe real-time interactions between Cas9–RNA and DNA targets and observes at least two different bound FRET states that may represent distinct steps in target search and proofreading.
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Quantitative analysis of multilayer organization of proteins and RNA in nuclear speckles at super resolution

TL;DR: Multi-color structured illumination microscopy imaging studies reveal a multilayer organization of nuclear speckles due to the interplay between favorable sequence-encoded intermolecular interactions of speckle-resident proteins and RNAs.
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Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation

TL;DR: The real-time dynamics of the L1 stalk, a structural element of the large ribosomal subunit that is implicated in directing tRNA movements during translation, are reported and a model for the release of E-site tRNA is suggested.