Issue 19, 2016

Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

Abstract

We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.

Graphical abstract: Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

  • This article is part of the themed collection: Foldamers

Supplementary files

Article information

Article type
Communication
Submitted
11 Janv. 2016
Accepted
02 Febr. 2016
First published
02 Febr. 2016

Chem. Commun., 2016,52, 3789-3792

Author version available

Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

N. A. Tavenor, Z. E. Reinert, G. A. Lengyel, B. D. Griffith and W. S. Horne, Chem. Commun., 2016, 52, 3789 DOI: 10.1039/C6CC00273K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements