4OZB

Backbone Modifications in the Protein GB1 Helix: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35

Summary for 4OZB

• Entry DOI: 10.2210/pdb4ozb/pdb
• Related: 4OZA 4OZC
• Descriptor: Streptococcal Protein GB1 Backbone Modified Variant: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35, GLYCEROL (3 entities in total)
• Functional Keywords: unnatural backbone, de novo protein
• Biological source: Streptococcus sp.
• Total number of polymer chains: 2
• Total formula weight: 12677.84

Authors

Reinert, Z.E.,Horne, W.S. (deposition date: 2014-02-14, release date: 2014-07-16, Last modification date: 2023-11-15)

Primary citation

Reinert, Z.E.,Horne, W.S.
Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
Chem Sci, 5:3325-3330, 2014

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: 25071931
DOI: 10.1039/C4SC01094A

Experimental method

X-RAY DIFFRACTION (1.8 Å)