期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 131, 期 39, 页码 14081-14087出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja9047575
关键词
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资金
- National Institutes of Health [GM 071589]
- National Science Foundation [CHE-0716126]
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 phosporylation 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.
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