4KGR

Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35

Summary for 4KGR

• Entry DOI: 10.2210/pdb4kgr/pdb
• Related: 4KGR 4KGS 4KGT
• Descriptor: Streptococcal Protein GB1 Backbone Modified Variant: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35, GLYCEROL (3 entities in total)
• Functional Keywords: unnatural backbone, de novo protein
• Total number of polymer chains: 8
• Total formula weight: 49994.29

Authors

Reinert, Z.E.,Lengyel, G.A.,Horne, W.S. (deposition date: 2013-04-29, release date: 2013-09-04, Last modification date: 2023-11-15)

Primary citation

Reinert, Z.E.,Lengyel, G.A.,Horne, W.S.
Protein-like Tertiary Folding Behavior from Heterogeneous Backbones.
J.Am.Chem.Soc., 135:12528-12531, 2013

PubMed Abstract: Because proteins play vital roles in life, much effort has been invested in their mimicry by synthetic agents. One approach is to design unnatural backbone oligomers ("foldamers") that fold like natural peptides. Despite success in secondary structure mimicry by such species, protein-like tertiary folds remain elusive. A fundamental challenge underlying this task is the design of a sequence of side chains that will specify a complex tertiary folding pattern on an unnatural backbone. We report here a sequence-based approach to convert a natural protein with a compact tertiary fold to an analogue with a backbone composed of ~20% unnatural building blocks but folding behavior similar to that of the parent protein.

PubMed: 23937097
DOI: 10.1021/ja405422v

Experimental method

X-RAY DIFFRACTION (2 Å)