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Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: Asp10Asn11 turnBackbone modifications in the inter-helix loop of designed miniprotein oPPalpha: Asp10Asn11 turn
Structural highlights
Publication Abstract from PubMedThe importance of beta-turns to protein folding has motivated extensive efforts to stabilize the motif with non-canonical backbone connectivity. Prior work has focused almost exclusively on turns between strands in a beta-sheet (i. e., hairpins). Turns in other structural contexts are also common in nature and have distinct conformational preferences; however, design principles for their mimicry remain poorly understood. Here, we report strategies that stabilize non-hairpin beta-turns through systematic evaluation of the impacts of backbone alteration on the high-resolution folded structure and folded stability of a helix-loop-helix prototype protein. Several well-established hairpin turn mimetics are shown detrimental to folded stability and/or hydrophobic core packing, while less-explored modification schemes that reinforce alternate turn types lead to improved stability and more faithful structural mimicry. Collectively, these results have implications in control over protein folding through chemical modification as well as the design of protein mimetics. Protein Backbone Alteration in Non-Hairpin beta-Turns: Impacts on Tertiary Folded Structure and Folded Stability.,Harmon TW, Horne WS Chembiochem. 2023 Jun 1;24(11):e202300113. doi: 10.1002/cbic.202300113. Epub 2023 , Mar 30. PMID:36920327[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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