Issue 29, 2014
From the journal:

Organic & Biomolecular Chemistry

Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation†

George A. Lengyel,a   Zachary E. Reinert,a   Brian D. Griffitha  and  W. Seth Horne*a  

* Corresponding authors

a Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA
E-mail: horne@pitt.edu

Abstract

The mimicry of protein tertiary structure by oligomers with unnatural backbones is a significant contemporary research challenge. Among common elements of secondary structure found in natural proteins, sheets have proven the most difficult to address. Here, we report the systematic comparison of different strategies for peptide backbone modification in β-sheets with the goal of identifying the best method for replacing a multi-stranded sheet in a protein tertiary fold. The most effective sheet modifications examined led to native-like tertiary folding behavior with a thermodynamic folded stability comparable to the prototype protein on which the modified backbones are based.

Graphical abstract: Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation

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Article information

DOI
https://doi.org/10.1039/C4OB00886C
Article type
Paper
Submitted
30 Apr 2014
Accepted
29 May 2014
First published
29 May 2014

Org. Biomol. Chem., 2014,12, 5375-5381

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Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation

G. A. Lengyel, Z. E. Reinert, B. D. Griffith and W. S. Horne, Org. Biomol. Chem., 2014, 12, 5375 DOI: 10.1039/C4OB00886C

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