ArticlePolymers2019
Chemically Denatured Structures of Porcine Pepsin using Small-Angle X-ray Scattering.
Article in Polymers, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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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Who cites it
2 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Recombinant subunits of SARS-CoV-2 spike protein as vaccine candidates to elicit neutralizing antibodies.Journal of clinical laboratory analysis · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Porcine pepsin is a gastric aspartic proteinase that reportedly plays a pivotal role in the digestive process of many vertebrates. We have investigated the three-dimensional (3D) structure and conformational transition of porcine pepsin in solution over a wide range of denaturant urea concentrations (0-10 M) using Raman spectroscopy and small-angle X-ray scattering. Furthermore, 3D GASBOR ab initio structural models, which provide an adequate conformational description of pepsin under varying denatured conditions, were successfully constructed. It was shown that pepsin molecules retain native conformation at 0-5 M urea, undergo partial denaturation at 6 M urea, and display a strongly unfolded conformation at 7-10 M urea. According to the resulting GASBOR solution models, we identified an intermediate pepsin conformation that was dominant during the early stage of denaturation. We believe that the structural evidence presented here provides useful insights into the relationship between enzymatic activity and conformation of porcine pepsin at different states of denaturation.
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