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Cuifeng Ying

As seen in: Nature, ACS Publications, BioRxiv
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Articles

Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins

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By Saaman Zargarbashi, Cyril Dominguez, Matthew Peters, Arman Yousefi, Yanhong Wang, Shreyasi Chatterjee, Andrew Hudson, Reuven Gordon, Christopher Mellor, Lei Xu, Mohsen Rahmani, Cuifeng Ying, Sharon Munday
| Nature Verified
Abstract Intrinsically disordered proteins (IDPs) and structured proteins with intrinsically disordered regions (IDRs) lack a definitive tertiary structure and contribute to the onset of diseases such as Alzheimer’s and cancer.
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Continuous, Low Latency Estimation of the Size and Shape of Single Proteins from Real-Time Nanopore Data

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By Yuanjie Li, Cuifeng Ying, Michael Mayer
Analytical Chemistry Cite this: Anal. Chem. 2025, XXXX, XXX Click to copy citationCitation copied! . This publication is licensed under CC-BY 4.0 . You are free to share (copy and redistribute) this article in any medium or format and to adapt (remix, transform, and build upon) the material for any purpose, even commercially within the parameters below: Creative Commons (CC): This is a Creative Commons license. Attribution (BY): Credit must be given to the creator.
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Continuous, Low Latency Estimation of the Size and Shape of Single Proteins from Real-Time Nanopore Data

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By Yuanjie Li, Cuifeng Ying, Michael Mayer
| BioRxiv
Abstract Existing approaches for nanopore sensing typically analyze resistive pulses from the translocation of individual proteins through the nanopore after completing the experiment. This approach foregoes instantaneous protein identification and precludes real-time experimental control. Here, we introduce a method for the analysis of real-time nanopore data capable of characterizing the size and approximate shape of proteins within a millisecond response time during data acquisition.
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