Structural Analysis of Protein Interfaces from 13C Direct-Detected Paramagnetic Relaxation Enhancements

被引：24

作者：

Madl, Tobias ^{[1
,2
]}

Felli, Isabella C. ^{[3
]}

Bertini, Ivano ^{[3
]}

Sattler, Michael ^{[1
,2
]}

机构：

[1] Helmholtz Zentrum Munchen, Inst Biol Struct, D-85764 Neuherberg, Germany

[2] Tech Univ Munich, Dept Chem, Munich Ctr Integrated Prot Sci & Chair Biomol NMR, D-85747 Garching, Germany

[3] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Sesto Fiorentino, Italy

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2010年 / 132卷 / 21期

基金：

奥地利科学基金会;

关键词：

PROTONLESS NMR-SPECTROSCOPY; GLOBAL FOLD DETERMINATION; BIOLOGICAL MACROMOLECULES; RESONANCE ASSIGNMENTS; SUPEROXIDE-DISMUTASE; COPPER(II) PROTEINS; MEMBRANE-PROTEINS; C-13-C-13; NOESY; CHEMICAL-SHIFT; HETERONUCLEAR;

D O I：

10.1021/ja1014508

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The measurement of C-13 directed-detected paramagnetic relaxation enhancements (PREs) on spin-labeled proteins combines the efficacy of PREs for the detection of long-range distance information with the favorable sensitivity and resolution of C-13 direct-detected experiments. The C-13 PREs provide long-range distance restraints to map binding interfaces in proteins and protein complexes and are especially useful for studies of high-molecular weight perdeuterated molecules.

引用

页码：7285 / +

页数：4

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