Sykes B D, Hull W E, Snyder G H
Biophys J. 1978 Feb;21(2):137-46. doi: 10.1016/S0006-3495(78)85514-3.
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.
本文给出了一系列分子量在6500至150000道尔顿范围内的蛋白质的质子核磁共振(NMR)自旋晶格弛豫时间(T1)和自旋-自旋弛豫时间(T2)测量结果。这些测量为交叉弛豫在蛋白质1H NMR T1测量中的作用提供了实验证据。讨论了这些测量结果与Kalk和Berendsen最近提出的理论之间的关系。结果表明,即使在相对较低的共振频率(如100 MHz)下,交叉弛豫在较大蛋白质的T1测量中也占主导地位。