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- W2509172455 startingPage "2804" @default.
- W2509172455 abstract "Transmembrane (TM) helices in integral membrane proteins are primarily α-helical in structure. Here we analyze 1134 TM helices in 90 high resolution membrane proteins and find that apart from the widely prevalent α-helices, TM regions also contain stretches of 310 (3 to 8 residues) and π-helices (5 to 19 residues) with distinct sequence signatures. The various helix perturbations in TM regions comprise of helices with kinked geometry, as well as those with an interspersed 310/π-helical fragment and show high occurrence in a few membrane proteins. Proline is frequently present at sites of these perturbations, but it is neither a necessary nor a sufficient requirement. Helix perturbations are also conserved within a family of membrane proteins despite low sequence identity in the perturbed region. Furthermore, a perturbation influences the geometry of the TM helix, mediates inter-helical interactions within and across protein chains and avoids hydrophobic mismatch of the helix termini with the bilayer. An analysis of π-helices in the TM regions of the heme copper oxidase superfamily shows that interspersed π-helices can vary in length from 6 to 19 amino acids or be entirely absent, depending upon the protein function. The results presented here would be helpful for prediction of 310 and π-helices in TM regions and can assist the computational design of membrane proteins." @default.
- W2509172455 created "2016-09-16" @default.
- W2509172455 creator A5013819419 @default.
- W2509172455 creator A5090518987 @default.
- W2509172455 date "2016-11-01" @default.
- W2509172455 modified "2023-09-29" @default.
- W2509172455 title "Helix perturbations in membrane proteins assist in inter-helical interactions and optimal helix positioning in the bilayer" @default.
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- W2509172455 doi "https://doi.org/10.1016/j.bbamem.2016.08.003" @default.
- W2509172455 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27521749" @default.
- W2509172455 hasPublicationYear "2016" @default.
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