7TIR

Backbone-modified variant of the B domain of Staphylococcal protein A: beta3-residues in helix 3

7TIR の概要

• エントリーDOI: 10.2210/pdb7tir/pdb
• 関連するPDBエントリー: 7TIO 7TIP 7TIQ 7TIS
• NMR情報: BMRB: 30983
• 分子名称: Immunoglobulin G binding protein A (1 entity in total)
• 機能のキーワード: de novo protein
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6673.37

構造登録者

Santhouse, J.R.,Leung, J.M.G.,Chong, L.T.,Horne, W.S. (登録日: 2022-01-14, 公開日: 2022-12-21, 最終更新日: 2023-11-15)

主引用文献

Santhouse, J.R.,Leung, J.M.G.,Chong, L.T.,Horne, W.S.
Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.
Chem Sci, 13:11798-11806, 2022

PubMed Abstract: Sequence-encoded folding is the foundation of protein structure and is also possible in synthetic chains of artificial chemical composition. In natural proteins, the characteristics of the unfolded state are as important as those of the folded state in determining folding energetics. While much is known about folded structures adopted by artificial protein-like chains, corresponding information about the unfolded states of these molecules is lacking. Here, we report the consequences of altered backbone composition on the structure, stability, and dynamics of the folded and unfolded states of a compact helix-rich protein. Characterization through a combination of biophysical experiments and atomistic simulation reveals effects of backbone modification that depend on both the type of artificial monomers employed and where they are applied in sequence. In general, introducing artificial connectivity in a way that reinforces characteristics of the unfolded state ensemble of the prototype natural protein minimizes the impact of chemical changes on folded stability. These findings have implications in the design of protein mimetics and provide an atomically detailed picture of the unfolded state of a natural protein and artificial analogues under non-denaturing conditions.

PubMed: 36320921
DOI: 10.1039/d2sc04427g

実験手法

SOLUTION NMR