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Biophysical Journal 21: 137-146 (1978)
© 1978 the Biophysical Society

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Experimental evidence for the role of cross-relaxation in proton nuclear magnetic resonance spin lattice relaxation time measurements in proteins.

B D Sykes, W E Hull and G H Snyder

ABSTRACT

Proton nuclear magnetic resonance (NMR) spin lattice relaxation time (T1) and spin-spin relaxation time (T2) measurements are presented for a number of proteins with molecular weights spanning the range of 6,500-150,000 daltons. These measurements provide experimental evidence for the role of cross-relaxation in 1H NMR T1 measurements in proteins. The relationship between these measurements and the theory recently presented by Kalk and Berendsen is discussed. The results indicate that cross-relaxation dominates the T1 measurements for the larger proteins, even at relatively low resonance frequencies such as 100 MHz.




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R. Gonzalez, H. Cheng, P Barnett, J Aguayo, B Glaser, B Rosen, C. Burt, and T Brady
Nuclear magnetic resonance imaging of the vitreous body
Science, January 27, 1984; 223(4634): 399 - 400.
[Abstract] [PDF]




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Copyright © 1978 by the Biophysical Society.