PEPTIDE & PROTEIN INTERACTIONS W/ METAL IONS

肽

• 批准号: 6118472
• 负责人: MICHAEL L GROSS
• 金额: $ 3.22万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-08-01 至 1999-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6118472
• 关键词: biological products; biomedical resource; proteins; spectrometry; technology /technique

We are investigating metal-ion interactions with peptides to measure relative metal-ion affinities of calcium with peptides that contain sequence motifs that are known to bind calcium. The interactions of Fe(II) with small peptides containing cysteine and Na(I) with cyclic peptides illustrate a second motivation whereby we seek new structural methods for biomolecules. The simple expedient of introducing a metal-cationized peptide or cyclic peptides is a means for taking "another look" at how a molecule fragments and determining its structure. The research has been extended to the protein calmodulin. We are developing a method to demonstrate that electrospray and H/D exchange can be used to follow Ca(II)-induced folding changes followed by noncovalent finding of calmodulin with hydrophobic peptides. The results serve as an appropriate demonstration of this relatively new capability of MS.

我们正在研究金属离子与肽的相互作用， 测量钙与肽的相对金属离子亲和力， 含有已知结合钙的序列基序。 的 Fe（II）与含有半胱氨酸的小肽的相互作用， Na（I）与环肽的反应说明了第二个动机， 寻找新的生物分子结构方法。 简单方便地 引入金属阳离子化的肽或环肽是一种手段， 以“另一种方式”观察分子是如何分裂的， 它的结构。 该研究已扩展到蛋白质钙调素。 我们 正在开发一种方法来证明电喷雾和H/D 交换可用于跟踪Ca（II）诱导的折叠变化， 通过与疏水肽的非共价发现钙调素。 的 结果作为一个适当的示范，这一相对较新的 MS的能力。