ArticleBiophysical journal2022
Insight into polyproline II helical bundle stability in an antifreeze protein denatured state.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Orientation affects hydrogen bonding cooperativity in polyproline II helical bundles.Communications chemistry · 2025Article
- Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins.Biophysical journal · 2025Article
- The Impact of Thermal and pH Variations on the Structure of Cathepsin D in the Hepatopancreas of Japanese Clam (Current protein & peptide science · 2025Article
- Hydrogen bonding patterns and cooperativity in polyproline II helical bundles.Communications chemistry · 2024Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The use of polyproline II (PPII) helices in protein design is currently hindered by limitations in our understanding of their conformational stability and folding. Recent studies of the snow flea antifreeze protein (sfAFP), a useful model system composed of six PPII helices, suggested that a low denatured state entropy contributes to folding thermodynamics. Here, circular dichroism spectroscopy revealed minor populations of PPII like conformers at low temperature. To get atomic level information on the conformational ensemble and entropy of the reduced, denatured state of sfAFP, we have analyzed its chemical shifts and {
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