ArticleBiophysical journal2021
Composition-dependent energetic contribution of complex salt bridges to collagen stability.
Article in Biophysical journal, 2021. 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.
- De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.Applied microbiology and biotechnology · 2025Article
- Stability of collagen heterotrimer with same charge pattern and different charged residue identities.Biophysical journal · 2023Article
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Authors and funding
4 authors.
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Abstract
Complex salt bridges, on which three or more charged residues interplay simultaneously, cannot be considered as addition of individual salt bridges. This is still an intriguing problem in protein folding and stability. Here, we used an obligated ABC-type collagen heterotrimer as a platform to study the relationship between energetic contributions and conformational details of three-body complex salt bridges anchored by positively charged residues, K and R. Eight complex salt bridges were constructed by engineering point mutations in the heterotrimer. The circular dichroism measurements showed that the K-anchored complex salt bridges were stronger than the R-anchored ones. The molecular dynamics simulation revealed that both types of salt bridges had distinct dynamic features. The energetic contribution of K-anchored salt bridges was mainly determined by strong single bridges. In the R-anchored complex salt bridges, both side-chain electrostatic interactions and side-chain-backbone hydrogen bonding were involved. An empirical equation was proposed to predict the energetic contributions with high accuracy (R
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