Consequences of incorporating thiaproline and its oxidized derivatives into collagen triple helices
Sign Up to like & getrecommendations! Published in 2023 at "Protein Science"
DOI: 10.1002/pro.4650
Abstract: (2R)‐4‐thiaproline (Thp) is an analog of proline, replacing Cγ in the pyrrolidine ring with sulfur. Its thiazolidine ring easily interconverts between endo and exo puckers due to a small energy barrier, which leads to destabilize… read more here.
Keywords: oxidized derivatives; derivatives collagen; thp; consequences incorporating ... See more keywords
Using a collagen heterotrimer to screen for cation-π interactions to stabilize triple helices
Sign Up to like & getrecommendations! Published in 2019 at "Chemical Physics Letters"
DOI: 10.1016/j.cplett.2018.10.073
Abstract: Abstract As one of non-covalent forces to stabilize protein, cation-π interactions in collagen have been received much attention. Three chains of collagen form its characteristic secondary structure, triple helices. Based on a collagen heterotrimer, abc,… read more here.
Keywords: cation interactions; triple helices; collagen heterotrimer; cation ... See more keywords
Covalent Capture of Collagen Triple Helices Using Lysine-Aspartate and Lysine-Glutamate Pairs.
Sign Up to like & getrecommendations! Published in 2020 at "Biomacromolecules"
DOI: 10.1021/acs.biomac.0c00878
Abstract: Collagen mimetic peptides (CMPs) self-assemble into a triple helix reproducing the most fundamental aspect of the collagen structural hierarchy. They are therefore important for both further understanding this complex family of proteins and use in… read more here.
Keywords: collagen; covalent capture; triple helices; structure ... See more keywords
Cation-π Interactions and Their Role in Assembling Collagen Triple Helices.
Sign Up to like & getrecommendations! Published in 2022 at "Biomacromolecules"
DOI: 10.1021/acs.biomac.2c00856
Abstract: Cation-π interactions play a significant role in the stabilization of globular proteins. However, their role in collagen triple helices is less well understood and they have rarely been used in de novo designed collagen mimetic… read more here.
Keywords: role; cation interactions; collagen triple; triple helices ... See more keywords
Hollow Octadecameric Self-Assembly of Collagen-like Peptides.
Sign Up to like & getrecommendations! Published in 2023 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.2c12931
Abstract: The folding of collagen is a hierarchical process that starts with three peptides associating into the characteristic triple helical fold. Depending on the specific collagen in question, these triple helices then assemble into bundles reminiscent… read more here.
Keywords: self assembly; hollow octadecameric; collagen; octadecameric self ... See more keywords
Predicting the stability of homotrimeric and heterotrimeric collagen helices
Sign Up to like & getrecommendations! Published in 2021 at "Nature Chemistry"
DOI: 10.1038/s41557-020-00626-6
Abstract: Robust methods for predicting thermal stabilities of collagen triple helices are critical for understanding natural structure and stability in the collagen family of proteins and also for designing synthetic peptides mimicking these essential proteins. In… read more here.
Keywords: collagen; predicting stability; collagen triple; triple helices ... See more keywords
Cryo-ET detects bundled triple helices but not ladders in meiotic budding yeast
Sign Up to like & getrecommendations! Published in 2022 at "PLoS ONE"
DOI: 10.1371/journal.pone.0266035
Abstract: In meiosis, cells undergo two sequential rounds of cell division, termed meiosis I and meiosis II. Textbook models of the meiosis I substage called pachytene show that nuclei have conspicuous 100-nm-wide, ladder-like synaptonemal complexes and… read more here.
Keywords: meiosis; cryo detects; triple helices; budding yeast ... See more keywords