ArticleProtein science : a publication of the Protein Society2022
Snapshots of urea-induced early structural changes and unfolding of an ankyrin repeat protein at atomic resolution.
Article in Protein science : a publication of the Protein Society, 2022. 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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1 citing paper in PubMed, 3 citations in OpenAlex.
- Snapshots of urea-induced early structural changes and unfolding of an ankyrin repeat protein at atomic resolution.Protein science : a publication of the Protein Society · 2022Article
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3 authors at 2 institutions in 3 countries.
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Abstract
Protein folding and unfolding is a complex process, underscored by the many proteotoxic diseases associated with misfolded proteins. Mapping pathways from a native structure to an unfolded protein or vice versa, identifying the intermediates, and defining the role of sequence and structure en route remain outstanding problems in the field. It is even more challenging to capture the events at atomistic resolution. X-ray diffraction has so far been used to understand how urea interacts with and unfolds two stable globular proteins. Here, we present the case study on PSMD10
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