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Issue 28, 2016
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Replacing a single atom accelerates the folding of a protein and increases its thermostability

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Abstract

The conformational attributes of proline can have a substantial effect on the folding of polypeptide chains into a native structure and on the stability of that structure. Replacing the 4S hydrogen of a proline residue with fluorine is known to elicit stereoelectronic effects that favor a cis peptide bond. Here, semisynthesis is used to replace a cis-proline residue in ribonuclease A with (2S,4S)-4-fluoroproline. This subtle substitution accelerates the folding of the polypeptide chain into its three-dimensional structure and increases the thermostability of that structure without compromising its catalytic activity. Thus, an appropriately situated fluorine can serve as a prosthetic atom in the context of a protein.

Graphical abstract: Replacing a single atom accelerates the folding of a protein and increases its thermostability

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Article information


Submitted
05 May 2016
Accepted
03 Jun 2016
First published
06 Jun 2016

Org. Biomol. Chem., 2016,14, 6780-6785
Article type
Paper

Replacing a single atom accelerates the folding of a protein and increases its thermostability

U. Arnold and R. T. Raines, Org. Biomol. Chem., 2016, 14, 6780
DOI: 10.1039/C6OB00980H

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