DEPT spectral editing in HCCONH-type experiments. Application to fast protein backbone and side chain assignment

被引：10

作者：

Brutscher, B ^{[1
]}

机构：

[1] UJF, CEA, CNRS, UMR 5075,Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble 1, France

来源：

JOURNAL OF MAGNETIC RESONANCE | 2004年 / 167卷 / 02期

关键词：

NMR; protein; reduced dimensionality; GFT; DEPT; spectral editing; resonance assignment;

D O I：

10.1016/j.jmr.2003.12.010

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

2D DEPT-(HCalpha,beta)-C-alpha,beta(CO)NH and 2D CT-DEPT-HC(CO)NH-TOCSY experiments are presented which allow fast resonance assignment of aliphatic protein side chains. In these 2D reduced-dimensionality experiments, two or three nuclei are frequency labeled in the indirect dimension. DEPT spectral editing reduces the number of correlation peaks detected in each 2D spectrum, and helps in amino-acid-type determination during sequential backbone resonance assignment. Applications are shown for a small 68-residue, and a highly deuterated 167-residue protein. The new experiments complement the set of 2D HNX correlation experiments, previously proposed for fast protein resonance assignment. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：178 / 184

页数：7

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