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半滤实验可用于分配、结构测定和水合分析未标记配体与 13C/15N 标记蛋白质的结合。

Half-filter experiments for assignment, structure determination and hydration analysis of unlabelled ligands bound to 13C/15N labelled proteins.

机构信息

NOVARTIS Pharma AG, CH-4002, Basel, Switzerland.

出版信息

J Biomol NMR. 1999 Jan;13(1):43-50. doi: 10.1023/A:1008345330011.

DOI:10.1023/A:1008345330011
PMID:21080262
Abstract

A novel variant of the 13C/15N ω2 half-filter experiment is reported for studying the hydration of an unlabelled ligand bound to a 15N and 13C uniformly labelled biological macromolecule. This doubly tuned filter experiment represents a powerful tool for obtaining resonance assignments, structure determination and hydration properties of a ligand. Its application to the binary complex formed by the inserted-domain (I-domain) of the leukocyte function-associated antigen-1 (LFA-1) with a ligand reveals the presence of H2O molecules at the binding interface.

摘要

报道了一种新型的 13C/15Nω2 半滤实验变体，用于研究与 15N 和 13C 均匀标记的生物大分子结合的未标记配体的水合作用。这种双调滤波器实验是获得配体的共振分配、结构确定和水合性质的有力工具。该实验应用于白细胞功能相关抗原-1（LFA-1）的插入结构域（I 结构域）与配体形成的二元复合物，揭示了结合界面处存在水分子。

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A (13)C double-filtered NOESY with strongly reduced artefacts and improved sensitivity.一种（13）C 双过滤 NOESY，具有明显减少的伪影和更高的灵敏度。
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