ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Enhancing protein stability through modifications to the N- and C-termini of natural proteins offers the distinct advantages of safety and cost-effectiveness when compared to the denovo design of proteins. To explore the effect of additional residues at the termini on protein stability, single-molecule magnetic tweezers are employed to examine the folding and unfolding dynamics of Cold Shock Protein (CSP) with various appended residues (LE-CSP-GS, KL-CSP-GS, KL-CSP-LE). The unfolding rate constant of the LE-CSP-GS is an order of magnitude faster than the others, while its folding rate constant decreased by more than an order of magnitude, resulting in upto ≈5 k
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Registered trials
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