6GWX

Stabilising and Understanding a Miniprotein by Rational Design.

6GWX の概要

• エントリーDOI: 10.2210/pdb6gwx/pdb
• 関連するPDBエントリー: 5LO2
• NMR情報: BMRB: 34295
• 分子名称: Optimised PPa-TYR (1 entity in total)
• 機能のキーワード: designed miniprotein ch-pi interactions weak non-covalent interactions in protiens solution structure proline-tyrosine interactions, structural 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

Porter Goff, K.L.,Williams, C.,Baker, E.G.,Nicol, D.,Samphire, J.L.,Zieleniewski, F.L.,Crump, M.P.,Woolfson, D.N. (登録日: 2018-06-26, 公開日: 2019-07-10, 最終更新日: 2024-11-20)

主引用文献

Porter Goff, K.L.,Nicol, D.,Williams, C.,Crump, M.P.,Zieleniewski, F.,Samphire, J.L.,Baker, E.G.,Woolfson, D.N.
Stabilizing and Understanding a Miniprotein by Rational Redesign.
Biochemistry, 58:3060-3064, 2019

PubMed Abstract: Miniproteins reduce the complexity of the protein-folding problem allowing systematic studies of contributions to protein folding and stabilization. Here, we describe the rational redesign of a miniprotein, PPα, comprising a polyproline II helix, a loop, and an α helix. The redesign provides a framework for interrogating noncovalent interactions. Optimized PPα has significantly improved thermal stability with a midpoint unfolding temperature () of 51 °C. Its nuclear magnetic resonance structure indicates a density of stabilizing noncovalent interactions that is higher than that of the parent peptide, specifically an increased number of CH-π interactions. In part, we attribute this to improved long-range electrostatic interactions between the two helical elements. We probe further sequence-stability relationships in the miniprotein through a series of rational mutations.

PubMed: 31251570
DOI: 10.1021/acs.biochem.9b00067

実験手法

SOLUTION NMR