ArticleProtein science : a publication of the Protein Society2012
A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Article
- Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Biophysical journal · 2016Review
- Acetone-Linked Peptides: A Convergent Approach for Peptide Macrocyclization and Labeling.Angewandte Chemie (International ed. in English) · 2015Article
- Simplified protein models: predicting folding pathways and structure using amino acid sequences.Physical review letters · 2013Article
- Atomic-level description of ubiquitin folding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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3 authors.
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Abstract
Using a combined crosslinking-ψ analysis strategy, we examine whether the structural content of the transition state of ubiquitin can be altered. A synthetic dichloroacetone crosslink is first introduced across two β strands. Whether the structural content in the transition state ensemble has shifted towards the region containing the crosslink is probed by remeasuring the ψ value at another region (ψ identifies the degree to which an inserted bi-Histidine metal ion binding site is formed in the transition state). For sites around the periphery of the obligate transition state nucleus, we find that the resulting changes in ψ values are near or at our detection limit, thereby indicating that the structural content of the transition state has not measurably changed upon crosslinking. This work demonstrates the utility of the simultaneous application of crosslinking and ψ-analysis for examining potential transition state heterogeneity in globular proteins.
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