Electrostatic interactions are one of the main factors influencing biomolecular conformation. The formation of noncovalent complexes by electrostatic interactions is governed by certain amino acid residues and post-translational modifications. It has been demonstrated that adjacent arginine forms noncovalent complex with phosphate; however, histidine noncovalent complexes have rarely been investigated. In the present work, we compare the interaction between basic epitopes (NLRRITRVN, SHHGLHSTPD) and diverse acidic and aromatic-rich peptides using both MALDI and ESI Mass spectrometry. We show that adjacent histidines can also form stable noncovalent bonds and that those bonds are probably formed by a salt bridge between the phosphate or the acid residues and the histidines. However, noncovalent complexes with the arginine epitopes form more readily and are stronger than those with histidine-containing epitopes.

中文翻译：

---

组氨酸，与精氨酸互动性较差的表亲

静电相互作用是影响生物分子构象的主要因素之一。通过静电相互作用形成的非共价复合物受某些氨基酸残基和翻译后修饰的控制。已经证明相邻的精氨酸与磷酸盐形成非共价复合物；然而，很少研究组氨酸非共价复合物。在目前的工作中，我们使用 MALDI 和 ESI 质谱法比较了碱性表位（NLRRITRVN、SHHGLHSTPD）与多种酸性和富含芳香族的肽之间的相互作用。我们表明相邻的组氨酸也可以形成稳定的非共价键，这些键可能是由磷酸盐或酸残基与组氨酸之间的盐桥形成的。然而，