4OZC
Backbone Modifications in the Protein GB1 Helix and Loops: beta-ACPC21, beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35, beta-ACPC40
4OZC の概要
エントリーDOI | 10.2210/pdb4ozc/pdb |
関連するPDBエントリー | 4OZA 4OZB |
分子名称 | Streptococcal Protein GB1 Backbone Modified Variant: beta-ACPC21, beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35, beta-ACPC40, SULFATE ION, GLYCEROL, ... (4 entities in total) |
機能のキーワード | unnatural backbone, de novo protein |
由来する生物種 | Streptococcus sp. |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 6539.11 |
構造登録者 | |
主引用文献 | Reinert, Z.E.,Horne, W.S. Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones. Chem Sci, 5:3325-3330, 2014 Cited by PubMed Abstract: The thermodynamics of protein folding are dictated by a complex interplay of interatomic interactions and physical forces. A variety of unnatural protein-like oligomers have the capacity to manifest defined folding patterns. While the energetics of folding in natural proteins is well studied, little is known about the forces that govern folding in modified backbones. Here, we explore the thermodynamic consequences of backbone alteration on protein folding, focusing on two types of chemical changes made in different structural contexts of a compact tertiary fold. Our results reveal a surprising favorable impact on folding entropy that accompanies modifications that increase disorder in the ensemble of unfolded states, due to differences in the solvation of natural and unnatural backbones. PubMed: 25071931DOI: 10.1039/C4SC01094A 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.301 Å) |
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