ArticlePloS one2021
Principal component analysis of alpha-helix deformations in transmembrane proteins.
Article in PloS one, 2021. 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.
- Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026Article
- Article
- Immunoinformatics-based design of a next generation multi-epitope vaccine candidate against Shigella boydii using a hierarchical subtractive proteomics approach.Scientific reports · 2025Article
- An integrated immunoinformatic approach to design a novel multiepitope chimeric vaccine againstFrontiers in immunology · 2025Article
- Immunoinformatics and Reverse Vaccinology Approach for the Identification of Potential Vaccine Candidates againstMicroorganisms · 2024Article
- Studying Conformational Properties of Transmembrane Domain of KCNE3 in a Lipid Bilayer Membrane Using Molecular Dynamics Simulations.Membranes · 2024Article
- Designing of a multi-epitopes based vaccine againstFrontiers in immunology · 2024Article
- Non-canonical helical transitions and conformational switching are associated with characteristic flexibility and disorder indices in TRP and Kv channels.Channels (Austin, Tex.) · 2023Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-helices are deformable secondary structural components regularly observed in protein folds. The overall flexibility of an α-helix can be resolved into constituent physical deformations such as bending in two orthogonal planes and twisting along the principal axis. We used Principal Component Analysis to identify and quantify the contribution of each of these dominant deformation modes in transmembrane α-helices, extramembrane α-helices, and α-helices in soluble proteins. Using three α-helical samples from Protein Data Bank entries spanning these three cellular contexts, we determined that the relative contributions of these modes towards total deformation are independent of the α-helix's surroundings. This conclusion is supported by the observation that the identities of the top three deformation modes, the scaling behaviours of mode eigenvalues as a function of α-helix length, and the percentage contribution of individual modes on total variance were comparable across all three α-helical samples. These findings highlight that α-helical deformations are independent of cellular location and will prove to be valuable in furthering the development of flexible templates in de novo protein design.
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