Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites

被引：54

作者：

Lippens, G

Wieruszeski, JM

Leroy, A

Smet, C

Sillen, A

Buée, L

Landrieu, I

机构：

[1] Univ Lille 2, CNRS, UMR 8525, Inst Pasteur, F-59019 Lille, France

[2] Univ Paris 11, Fac Pharm, Lab Biochim Appl, F-92296 Chatenay Malabry, France

[3] Inst Med Predictive & Rech Therapeut, INSERM, U422, F-59045 Lille, France

来源：

CHEMBIOCHEM | 2004年 / 5卷 / 01期

关键词：

NMR spectroscopy; phosphorylation; proline; protein structures; Tau protein;

D O I：

10.1002/cbic.200300763

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

NMR spectroscopy of the full-length neuronal Tau protein has proved to be difficult due to the length of the protein and the unfavorable amino acid composition. We show that the random-coil chemical shift values and their dependence on the presence of a proline residue in the (i + 1) position can successfully be exploited to assign all proline-directed phosphorylation sites. This is a first step toward the study of the phosphorylation of Tau by NMR spectroscopy.

引用

页码：73 / 78

页数：6

共 15 条

[1] Role of phosphorylation in the conformation of τ peptides implicated in Alzheimer's disease [J].