ArticleProtein science : a publication of the Protein Society2023
Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 4 citations in OpenAlex.
- Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.Angewandte Chemie (International ed. in English) · 2026Article
- GRAMMCell: Docking-based Cell Modeling Resource.Journal of molecular biology · 2025Article
- Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
4 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Slow conformational changes are often directly linked to protein function. It is however less clear how such processes may perturb the overall folding stability of a protein. We previously found that the stabilizing double mutant L49I/I57V in the small protein chymotrypsin inhibitor 2 from barley led to distributed increased nanosecond and faster dynamics. Here we asked what effects the L49I and I57V substitutions, either individually or together, have on the slow conformational dynamics of CI2. We used
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