ArticleJournal of molecular modeling2013
Hypothetical in silico model of the early-stage intermediate in protein folding.
Article in Journal of molecular modeling, 2013. 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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Who cites it
3 citing papers in PubMed.
- Different Synergy in Amyloids and Biologically Active Forms of Proteins.International journal of molecular sciences · 2019Article
- Statistical dictionaries for hypothetical in silico model of the early-stage intermediate in protein folding.Journal of computer-aided molecular design · 2015Article
- Contingency Table Browser - prediction of early stage protein structure.Bioinformation · 2015Article
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Authors and funding
5 authors.
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Abstract
This paper presents a method for determining the structure of the early stage (ES) intermediate in the multistage protein folding process. ES structure is modeled on the basis of a limited conformational subspace of the Ramachandran plot. The model distinguishes seven structural motifs corresponding to seven local probability maxima within the limited conformational subspace. Three of these are assigned to well-defined secondary structures, while the remaining four are found to represent various types of random coils. The presented heuristic approach also provides insight into the reasons behind incorrect predictions occurring when the folding process depends on external factors (e.g., ligands, ions or other proteins) rather than on the characteristics of the backbone itself. The accuracy of the presented method is estimated at around 48 %.
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