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Evidence for dynamics on a 100 ns time scale from single- and double-quantum nitrogen-14 NMR in solid peptides
被引:27
作者:

Cavadini, Simone
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Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland

Abraham, Anuji
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Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland

Ulzega, Simone
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Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland

Bodenhausen, Geoffrey
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Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland
Ecole Normale Super, CNRS, Dept Chim, F-75231 Paris 05, France Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland
机构:
[1] Ecole Polytech Fed Lausanne, Lab Resonance Magnet Biomol, CH-1015 Lausanne, Switzerland
[2] Ecole Normale Super, CNRS, Dept Chim, F-75231 Paris 05, France
关键词:
D O I:
10.1021/ja802603q
中图分类号:
O6 [化学];
学科分类号:
0703 ;
摘要:
The indirect detection of N-14 spectra via protons in the manner of heteronuclear multiple-quantum correlation (HMQC) allows one to obtain single- (SQ) and double-quantum (DQ) N-14 spectra in solids. A comparison of the SQ and DQ line widths as a function of temperature with simulations reveals motions in the tripeptide AAG with rates on the order of 10(7) s(-1) at 49 degrees C.
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页码:10850 / +
页数:3
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