The characterization of weak protein-protein interactions: Evidence from DEER for the trimerization of a von Willebrand factor A domain in solution

被引:54
作者
Jeschke, G
Abbott, RJM
Lea, SM
Timmel, CR
Banham, JE
机构
[1] Max Planck Inst Polymer Res, D-55021 Mainz, Germany
[2] Univ Oxford, Dept Biochem, Mol Biophys Lab, Oxford OX1 3QU, England
[3] Univ Oxford, Inorgan Chem Lab, Oxford OX1 3QR, England
[4] Univ Oxford, Phys & Theoret Chem Lab, Oxford OX1 3QR, England
关键词
DEER; EPR spectroscopy; noncovalent interactions; proteins; structure elucidation;
D O I
10.1002/anie.200503720
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
(Figure Presented) Distance determination: A double electron electron resonance (DEER) measurement of a distance of 6.1 nm (green lines) between singly nitroxide-labeled human von Willebrand Factor A domains demonstrates oligomerization of this domain in dilute solution (see structure); probably in an arrangement similar to that observed in the crystal structure. The DEER technique should be generally applicable for characterizing noncovalent interactions between macromolecules in solution. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:1058 / 1061
页数:4
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