H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins

被引：77

作者：

Bermel, Wolfgang ^{[3
]}

Bertini, Ivano ^{[1
,2
]}

Csizmok, Veronika ^{[4
]}

Felli, Isabella C. ^{[1
,2
]}

Pierattelli, Roberta ^{[1
,2
]}

Tompa, Peter ^{[4
]}

机构：

[1] Univ Florence, CERM, IT-50019 Florence, Italy

[2] Univ Florence, Dept Chem, IT-50019 Florence, Italy

[3] Bruker BioSpin GmbH, D-76287 Rheinstetten, Germany

[4] Hungarian Acad Sci, Biol Res Ctr, Inst Enzymol, H-1113 Budapest, Hungary

来源：

JOURNAL OF MAGNETIC RESONANCE | 2009年 / 198卷 / 02期

关键词：

C-13 direct detection; Protonless NMR; Intrinsically disordered proteins; Virtual decoupling; IPAP; Spin-state selection; PROTONLESS NMR; UNSTRUCTURED PROTEINS; POLARIZATION TRANSFER; COMPLETE ASSIGNMENT; UNFOLDED PROTEINS; CHEMICAL-SHIFTS; SEQUENCE; NUCLEI; ENHANCEMENT; DATABASE;

D O I：

10.1016/j.jmr.2009.02.012

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Here, we present a series of exclusively heteronuclear multidimensional NMR experiments, based on C-13 direct detection, which exploit the H-1 polarization as a starting source to increase the signal-to-noise ratio. This contributes to make this spectroscopy more useful and usable. Examples are reported for a suitable system such as securin, an intrinsically disordered protein of 22 kDa. (C) 2009 Elsevier Inc. All rights reserved.

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页码：275 / 281

页数：7

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