Isotope-filtered affinity NMR

被引：29

作者：

Gonnella, N

Lin, MF

Shapiro, MJ

Wareing, JR

Zhang, XL

机构：

[1] Novartis Pharmaceut Corp, Dept Analyt, Summit, NJ 07901 USA

[2] Novartis Pharmaceut Corp, Dept Prot Struct, Summit, NJ 07901 USA

[3] Novartis Pharmaceut Corp, Dept Metab & Cardiovasc Dis, Preclin Res, Summit, NJ 07901 USA

来源：

JOURNAL OF MAGNETIC RESONANCE | 1998年 / 131卷 / 02期

关键词：

diffusion NMR; affinity NMR; C-13 isotope editing; pulse sequence; protein binding;

D O I：

10.1006/jmre.1997.1376

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A double-editing pulse sequence has been developed that allows the direct observation of protein binding ligand(s) from a mixture of compounds. This technique should aid the discovery of lead pharmaceutical compounds. The proton NMR signals from protein and the nonbinding ligands are simultaneously eliminated using C-13 isotope editing and PFG diffusion-edited NMR. This new experiment is demonstrated using C-13/N-15-labeled stromelysin catalytic domain (SCD). (C) 1998 Academic Press.

引用

收藏

页码：336 / 338

页数：3

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