8ERY

Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: Asp10Asn11 turn

8ERY の概要

• エントリーDOI: 10.2210/pdb8ery/pdb
• NMR情報: BMRB: 31048
• 分子名称: Designed miniprotein oPPalpha: Asp10Asn11 turn (1 entity in total)
• 機能のキーワード: protein mimetic, heterogeneous backbone, de novo protein
• 由来する生物種: Streptococcus mutans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3791.35

構造登録者

Harmon, T.W.,Horne, W.S. (登録日: 2022-10-13, 公開日: 2023-04-05, 最終更新日: 2024-10-16)

主引用文献

Harmon, T.W.,Horne, W.S.
Protein Backbone Alteration in Non-hairpin beta-Turns: Impacts on Tertiary Folded Structure and Folded Stability.
Chembiochem, :e202300113-e202300113, 2023

PubMed Abstract: The importance of β-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 β-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 β-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.

PubMed: 36920327
DOI: 10.1002/cbic.202300113

実験手法

SOLUTION NMR