Abstract Refractile bodies (R-bodies) are protein assemblies that form intracellular rolls and extend into spirals in response to environmental stimuli. Type 51 R-body assembles from four Reb proteins and undergoes rapid, repeatable ∼50-fold extension. Although R-bodies were described more than 70 years ago, the roles of RebC and RebD remained unclear, whereas RebA and RebB are proposed as major components. Here, we characterize the wild-type R-body (Rb_WT) and reb gene knockout mutants using integrated biophysical analyses. RebD was incorporated as a minor component, whereas RebC was not detectably incorporated into the final assembly. Mutants lacking RebA or RebB formed rolls but lost pH-dependent extension and the ordered lamellar architecture characteristic of Rb_WT. In contrast, mutants lacking RebC and/or RebD exhibited reduced roll formation and formed β-sheet-rich aggregation. Thus, pH-responsive actuation is dictated not simply by major architectural components alone, but by a regulated assembly pathway that builds the ordered lamellar architecture.
The comparison of adopter and non-adopter sample reveals three potential adoption inhibitor, security, data privacy, and portability, which underlines the importance of the technical and security perspectives for research investigating the adoption of technology.
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Anh Nguyen-Duc, Xiaofeng Wang, P. Abrahamsson· International Conference on...· 44 citations· ⚡5
It is demonstrated that linker-free PROTACs can outperform traditional designs, marking a paradigm shift in PROTAC development for targeted protein degradation.
Pinal, a 16-billion-parameter foundation model that produces protein candidates from natural-language functional descriptions, supports natural language as a high-level interface for candidate generation in protein design, enabling programmable exploration with reduced reliance on manually specified structural or seque...
A new machine-learning framework aims to improve the success rate of computational protein design while moving away from results that reproduce sequences found in nature.