ArticleInternational journal of proteomics2014
The influence of flanking secondary structures on amino Acid content and typical lengths of 3/10 helices.
Article in International journal of proteomics, 2014. 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.
- The Activity of the Durum Wheat (Antioxidants (Basel, Switzerland) · 2022Article
- Wenxiang 3.0: Evolutionary Visualization of α, π, and 3/10 Helices.Evolutionary bioinformatics online · 2022Review
- Article
- Evaluation of peptide designing strategy against subunit reassociation in mucin 1: A steered molecular dynamics approach.PloS one · 2017Article
- Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric Strain.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
We used 3D structures of a highly redundant set of bacterial proteins encoded by genes of high, average, and low GC-content. Four types of connecting bridges-regions situated between any of two major elements of secondary structure (alpha helices and beta strands)-containing a pure random coil were compared with connecting bridges containing 3/10 helices. We included discovered trends in the original "VVTAK Connecting Bridges" algorithm, which is able to predict more probable conformation for a given connecting bridge. The highest number of significant differences in amino acid usage was found between 3/10 helices containing bridges connecting two beta strands (they have increased Phe, Tyr, Met, Ile, Leu, Val, and His usages but decreased usages of Asp, Asn, Gly, and Pro) and those without 3/10 helices. The typical (most common) length of 3/10 helices situated between two beta strands and between beta strand and alpha helix is equal to 5 amino acid residues. The preferred length of 3/10 helices situated between alpha helix and beta strand is equal to 3 residues. For 3/10 helices situated between two alpha helices, both lengths (3 and 5 amino acid residues) are typical.
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Registered trials
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