THE EFFECTS OF PROTEINS ON THE PROTON NMR TRANSVERSE RELAXATION-TIMES OF WATER .1. NATIVE BOVINE SERUM-ALBUMIN
THE EFFECTS OF PROTEINS ON THE PROTON NMR TRANSVERSE RELAXATION-TIMES OF WATER .1. NATIVE BOVINE SERUM-ALBUMIN
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DOI：
10.1080/00268978900101531
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发表时间：
1989-07-01
影响因子：
1.7
通讯作者：
BELTON, PS
中科院分区：
文献类型：
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作者：
HILLS, BP;TAKACS, SF;BELTON, PS
天然牛血清白蛋白溶液中水质子横向弛豫的主要特征可以用水和蛋白质质子之间的快速化学交换来定量解释。横向质子弛豫色散是CPMG脉冲间隔和光谱仪频率的函数，与蛋白质中氨基酸侧链的NH和OH质子与水的快速交换一致。平均一阶汇率约为5 × 103s-1。尽管有证据表明蛋白质影响其周围水的状态（所谓的“结合水”概念），但获得的结果表明，与化学交换机制的强大影响相比，这对质子弛豫的影响较小。
The major features of N.M.R. transverse water proton relaxation in solutions of native bovine serum albumin can be quantitatively interpreted in terms of fast chemical exchange between water and protein protons. Transverse proton relaxation dispersions are observed as a function of CPMG pulse spacing and spectrometer frequency and are shown to be consistent with the fast exchange of water with NH and OH protons of the amino acid side chains in the protein. The mean first order exchange rate is about 5 × 103s-1. Although there is evidence that proteins influence the state of the water around them (the so called ‘bound’ water concept) the results obtained suggest that this influences the proton relaxation in a minor way compared to the potent effect of the chemical exchange mechanism.