Evidence for dynamics on a 100 ns time scale from single- and double-quantum nitrogen-14 NMR in solid peptides.
The indirect detection of 14N spectra via protons in the manner of heteronuclear multiple-quantum correlation (HMQC) allows one to obtain single- (SQ) and double-quantum (DQ) 14N 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 107 s(-1) at 49 degrees C.
Cavadini
Simone
S
Laboratoire de Résonance Magnétique Biomoléculaire, Ecole Polytechnique Fédérale de Lausanne, Batochime, CH-1015 Lausanne, Switzerland.
Abraham
Anuji
A
Ulzega
Simone
S
Bodenhausen
Geoffrey
G
D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards; D008956:Models, Chemical; D009584:Nitrogen / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D011522:Protons; D011789:Quantum Theory; D012015:Reference Standards; D013816:Thermodynamics; D013997:Time Factors
D009842:Oligopeptides; D011522:Protons; D009584:Nitrogen