| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 21: 137-146 (1978)
© 1978 the Biophysical Society
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.
This article has been cited by other articles:
![]() |
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] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |