13C APSY-NMR for sequential assignment of intrinsically disordered proteins

被引：17

作者：

Murrali, Maria Grazia ^{[1
]}

Schiavina, Marco ^{[1
]}

Sainati, Valerio ^{[1
]}

Bermel, Wolfgang ^{[2
]}

Pierattelli, Roberta ^{[1
,3
]}

Felli, Isabella C. ^{[1
,3
]}

机构：

[1] Univ Florence, CERM, Via Luigi Sacconi 6, I-50019 Florence, Italy

[2] Bruker BioSpin GmbH, D-76287 Silberstreifen, Rheinstetten, Germany

[3] Univ Florence, Dept Chem Ugo Schiff, I-50019 Florence, Italy

来源：

JOURNAL OF BIOMOLECULAR NMR | 2018年 / 70卷 / 03期

关键词：

Intrinsically disordered proteins; IDPs; Assignment; NUS; C-13; detection; AUTOMATED PROJECTION SPECTROSCOPY; MULTIDIMENSIONAL NMR; RECONSTRUCTION; EXTENSION; DYNAMICS;

D O I：

10.1007/s10858-018-0167-4

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：

The increasingly recognized biological relevance of intrinsically disordered proteins requires a continuous expansion of the tools for their characterization via NMR spectroscopy, the only technique so far able to provide atomic-resolution information on these highly mobile macromolecules. Here we present the implementation of projection spectroscopy in C-13-direct detected NMR experiments to achieve the sequence specific assignment of IDPs. The approach was used to obtain the complete backbone assignment at high temperature of alpha-synuclein, a paradigmatic intrinsically disordered protein.

引用

页码：167 / 175

页数：9

共 53 条

[51] A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins [J].