Frequency selective heteronuclear dipolar recoupling in rotating solids:: Accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides

被引:235
作者
Jaroniec, CP
Tounge, BA
Herzfeld, J
Griffin, RG [1 ]
机构
[1] MIT, Dept Chem, Cambridge, MA 02139 USA
[2] MIT, Francis Bitter Natl Magnet Lab, Cambridge, MA 02139 USA
[3] Brandeis Univ, Keck Inst Cellular Visualizat, Waltham, MA 02454 USA
[4] Brandeis Univ, Dept Chem, Waltham, MA 02454 USA
关键词
D O I
10.1021/ja003266e
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We describe a magic-angle spinning NMR experiment for selective C-13-N-15 distance measurements in uniformly C-13,N-15-labeled solids, where multiple C-13-N-15 and C-13-C-13 interactions complicate the accurate measurement of structurally interesting, weak C-13-N-15 dipolar couplings. The new experiment, termed FSR (frequency selective REDOR), combines the REDOR pulse sequence with a frequency selective spin-echo to recouple a single C-13-N-15 dipolar interaction in a multiple spin system. Concurrently the remaining C-13-N-15 dipolar couplings and all C-13-C-13 scalar couplings to the selected C-13 are suppressed. The C-13-N-15 coupling of interest is extracted by a least-squares fit of the experimentally observed modulation of the C-13 spin-echo intensity to the analytical expression describing the dipolar dephasing in an isolated heteronuclear spin pair under conventional REDOR. The experiment is demonstrated in three uniformly C-13,N-15-labeled model systems: asparagine, N-acetyl-L-Val-L-Leu acid N-formyl-L-Met-L-Leu-L-Phe; in N-formyl-[U-C-13,N-15]L-Met-L-Leu-L-Phe we have determined a total of 16 internuclear distances in the 2.5-6 Angstrom range.
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页码:3507 / 3519
页数:13
相关论文
共 80 条
[1]   NUCLEAR MAGNETIC RESONANCE SPECTRA FROM A CRYSTAL ROTATED AT HIGH SPEED [J].
ANDREW, ER ;
BRADBURY, A ;
EADES, RG .
NATURE, 1958, 182 (4650) :1659-1659
[2]  
[Anonymous], 1997, SPIN CHOREOGRAPHY BA
[3]  
[Anonymous], 2018, Protein nmr spectroscopy: principles and practice
[4]   Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils [J].
Antzutkin, ON ;
Balbach, JJ ;
Leapman, RD ;
Rizzo, NW ;
Reed, J ;
Tycko, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (24) :13045-13050
[5]   SIMPSON: A general simulation program for solid-state NMR spectroscopy [J].
Bak, M ;
Rasmussen, JT ;
Nielsen, NC .
JOURNAL OF MAGNETIC RESONANCE, 2000, 147 (02) :296-330
[6]   Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR [J].
Balbach, JJ ;
Ishii, Y ;
Antzutkin, ON ;
Leapman, RD ;
Rizzo, NW ;
Dyda, F ;
Reed, J ;
Tycko, R .
BIOCHEMISTRY, 2000, 39 (45) :13748-13759
[7]  
BAX A, 1980, 2 DIMENSIONAL NUCL M
[8]   HETERONUCLEAR DECOUPLING IN ROTATING SOLIDS [J].
BENNETT, AE ;
RIENSTRA, CM ;
AUGER, M ;
LAKSHMI, KV ;
GRIFFIN, RG .
JOURNAL OF CHEMICAL PHYSICS, 1995, 103 (16) :6951-6958
[9]   Homonuclear radio frequency-driven recoupling in rotating solids [J].
Bennett, AE ;
Rienstra, CM ;
Griffiths, JM ;
Zhen, WG ;
Lansbury, PT ;
Griffin, RG .
JOURNAL OF CHEMICAL PHYSICS, 1998, 108 (22) :9463-9479
[10]   Frequency-selective heteronuclear dephasing by dipole couplings in spinning and static solids [J].
Bennett, AE ;
Rienstra, CM ;
Lansbury, PT ;
Griffin, RG .
JOURNAL OF CHEMICAL PHYSICS, 1996, 105 (23) :10289-10299