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交叉弛豫在蛋白质质子核磁共振自旋晶格弛豫时间测量中的作用的实验证据。

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

作者信息

Sykes B D, Hull W E, Snyder G H

出版信息

Biophys J. 1978 Feb;21(2):137-46. doi: 10.1016/S0006-3495(78)85514-3.

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.

摘要

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。

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