Work

Controlling Peptide Folding with Repulsive Interactions between Phosphorylated Amino Acids and Tryptophan

Year: 2009

Type: article

Abstract: Phosphorylated amino acids were incorporated into a designed beta-hairpin peptide to study the effect on beta-hairpin structure when the phosphate group is positioned to interact with a tryptophan residue on the neighboring strand. The three commonly phosphorylated residues in biological systems, serine, threonine, and tyrosine, were studied in the same beta-hairpin system. It was found that phosphorylation destabilizes the hairpin structure by approximately 1.0 kcal/mol, regardless of the type of phosphorylated residue. In contrast, destabilization due to glutamic acid was about 0.3 kcal/mol. Double mutant cycles and pH studies are consistent with a repulsive interaction as the source of destabilization. These findings demonstrate a novel mechanism by which phosphorylation may influence protein structure and function.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja9047575

Authors: Alexander J. Riemen, Marcey L. Waters

Institution: University of North Carolina at Chapel Hill

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, Division of Chemistry

Awards: G1303025848, G7051052955