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
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
收藏
页码:178 / 184
页数:7
相关论文
共 36 条
  • [1] EDITING OF C-13 NMR-SPECTRA - A PULSE SEQUENCE FOR THE GENERATION OF SUBSPECTRA
    BENDALL, MR
    DODDRELL, DM
    PEGG, DT
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1981, 103 (15) : 4603 - 4605
  • [2] Optimized set of two-dimensional experiments for fast sequential assignment, secondary structure determination, and backbone fold validation of 13C/15N-labelled proteins
    Bersch, B
    Rossy, E
    Covès, J
    Brutscher, B
    [J]. JOURNAL OF BIOMOLECULAR NMR, 2003, 27 (01) : 57 - 67
  • [3] DETERMINATION OF AN INITIAL SET OF NOE-DERIVED DISTANCE CONSTRAINTS FOR THE STRUCTURE DETERMINATION OF N-15/C-13-LABELED PROTEINS
    BRUTSCHER, B
    MORELLE, N
    CORDIER, F
    MARION, D
    [J]. JOURNAL OF MAGNETIC RESONANCE SERIES B, 1995, 109 (02): : 238 - 242
  • [4] BRUTSCHER B, 1995, J BIOMOL NMR, V5, P202, DOI 10.1007/BF00208811
  • [5] DESIGN OF A COMPLETE SET OF 2-DIMENSIONAL TRIPLE-RESONANCE EXPERIMENTS FOR ASSIGNING LABELED PROTEINS
    BRUTSCHER, B
    SIMORRE, JP
    CAFFREY, MS
    MARION, D
    [J]. JOURNAL OF MAGNETIC RESONANCE SERIES B, 1994, 105 (01): : 77 - 82
  • [6] BRUTSCHER B, IN PRESS J BIOMOL NM
  • [7] Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain
    Champier, L
    Sibille, N
    Bersch, B
    Brutscher, B
    Blackledge, M
    Covès, J
    [J]. BIOCHEMISTRY, 2002, 41 (11) : 3770 - 3780
  • [8] Protein structure determination using molecular fragment replacement and NMR dipolar couplings
    Delaglio, F
    Kontaxis, G
    Bax, A
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (09) : 2142 - 2143
  • [9] Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins
    Ding, KY
    Gronenborn, AM
    [J]. JOURNAL OF MAGNETIC RESONANCE, 2002, 156 (02) : 262 - 268
  • [10] Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
    Gardner, KH
    Rosen, MK
    Kay, LE
    [J]. BIOCHEMISTRY, 1997, 36 (06) : 1389 - 1401