ArticleThe protein journal2009
A reexamination of correlations of amino acids with particular secondary structures.
Article in The protein journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Influence of hydrophobicity on the antimicrobial activity of helical antimicrobial peptides: a study focusing on three mastoparans.Molecular diversity · 2025Article
- Functional Characterization of SixMolecular pharmaceutics · 2023Article
- Peptide-Based Vaccine against SARS-CoV-2: Peptide Antigen Discovery and Screening of Adjuvant Systems.Pharmaceutics · 2022Article
- The acidic tail of HMGB1 regulates its secondary structure and conformational flexibility: A circular dichroism and molecular dynamics simulation study.Computational and structural biotechnology journal · 2020Article
- Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Nucleic acids research · 2017Article
- The Purine Bias of Coding Sequences is Determined by Physicochemical Constraints on Proteins.Bioinformatics and biology insights · 2014Article
- β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides.PloS one · 2014Article
- Effect of codon message on xylanase thermal activity.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using the data from Protein Data Bank the correlations of primary and secondary structures of proteins were analyzed. The correlation values of the amino acids and the eight secondary structure types were calculated, where the position of the amino acid and the position in sequence with the particular secondary structure differ at most 25. The diagrams describing these results indicate that correlations are significant at distances between -9 and 10. The results show that the substituents on Cbeta or Cgamma atoms of amino acid play major role in their preference for particular secondary structure at the same position in the sequence, while the polarity of amino acid has significant influence on alpha-helices and strands at some distance in the sequence. The diagrams corresponding to polar amino acids are noticeably asymmetric. The diagrams point out the exchangeability of residues in the proteins; the amino acids with similar diagrams have similar local folding requirements.
Indexed as
Identifiers
19280326What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.