Document Type
Article Presentation
Original Publication Date
2026
Date of Submission
October 2026
Abstract
This presentation goes over the PUFF algorithm, Protein Unfolding/Folding Frameworks, based on using amino acid sequences to detect prions. It was found that there are bimodal characteristics found in most vertebrate and yeast prions. PUFF was used to predict the intrinsically disordered and folded regions specifically within the E. coli proteome. From the criterion, PUFF was able to predict 102 novel 1st-generation prions, and with further analysis with subcellular compartmentalization and tryptophan distribution, it was able to establish a group of 6 cytoplasmic 2nd-generation prion candidates. The study enhanced the understanding of E. coli's genome nature and offers a new strategy to help identify prions.
Recommended Citation
Shreeve, Katherine & Jang, Jinoh & Srivathsan, Mridula & Li, Siyu & Scott, Taylor & Cavagnero, Silvia. (2026). Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics. Proteins: Structure, Function, and Bioinformatics. n/a-n/a. 10.1002/prot.70171.
Rights
© The Author(s)