Structural highlights
Publication Abstract from PubMed
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 approximately 20% unnatural building blocks but folding behavior similar to that of the parent protein.
Protein-like Tertiary Folding Behavior from Heterogeneous Backbones.,Reinert ZE, Lengyel GA, Horne WS J Am Chem Soc. 2013 Aug 28;135(34):12528-31. doi: 10.1021/ja405422v. Epub 2013, Aug 15. PMID:23937097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Reinert ZE, Lengyel GA, Horne WS. Protein-like Tertiary Folding Behavior from Heterogeneous Backbones. J Am Chem Soc. 2013 Aug 28;135(34):12528-31. doi: 10.1021/ja405422v. Epub 2013, Aug 15. PMID:23937097 doi:10.1021/ja405422v
