CERM and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino (Florence), Italy.
Bruker BioSpin GmbH, Silberstreifen, 76287, Rheinstetten, Germany.
Chembiochem. 2018 Aug 6;19(15):1625-1629. doi: 10.1002/cbic.201800172. Epub 2018 Jun 21.
NMR spectroscopy is one of the main techniques used for high-resolution studies of intrinsically disordered proteins (IDPs), permitting mapping of the structural and dynamic features of all the amino acids constituting the polypeptide at atomic resolution. Only proline residues are less straightforward to characterize because they lack any amide proton, thus rendering them not directly visible in the commonly used 2D H, N correlation experiments. However, proline residues are highly abundant in IDPs and can mediate important functions. In this work we present an easy and effective way to obtain fingerprints of proline residues in IDPs at high resolution.
NMR 光谱学是用于高分辨率研究无规卷曲蛋白质（IDPs）的主要技术之一，它可以在原子分辨率下绘制构成多肽的所有氨基酸的结构和动态特征图。只有脯氨酸残基的特征描述不太直接，因为它们缺乏任何酰胺质子，因此在常用的 2D H、N 相关实验中它们无法直接显现。然而，脯氨酸残基在 IDPs 中含量非常丰富，并且可以介导重要功能。在这项工作中，我们提出了一种在高分辨率下获得 IDPs 中脯氨酸残基指纹图谱的简单有效的方法。
