Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophan.
Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophan.
复制标题
通过磷酸化氨基酸和色氨酸之间的排斥相互作用控制肽折叠。
DOI：
10.1021/ja9047575
复制
发表时间：
2009
影响因子：
15
通讯作者：
Waters,MarceyL
中科院分区：
文献类型：
--
作者：
Riemen,AlexanderJ;Waters,MarceyL
将磷酸化氨基酸掺入设计的β-发夹肽中，以研究当磷酸基团定位成与相邻链上的色氨酸残基相互作用时对β-发夹结构的影响。在相同的β-发夹系统中研究了生物系统中三种常见的磷酸化残基，丝氨酸、苏氨酸和酪氨酸。发现磷酸化使发夹结构不稳定约1.0 kcal/mol，而与磷酸化残基的类型无关。相比之下，谷氨酸引起的去稳定化约为0.3 kcal/mol。双突变体循环和pH值的研究是一致的排斥相互作用的来源不稳定。这些发现证明了磷酸化可能影响蛋白质结构和功能的新机制。
Phosphorylated amino acids were incorporated into a designed β-hairpin peptide to study the effect on β-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 β-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.