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Multidimensional cross-correlation relaxometry of aqueous protein systems

机译：水性蛋白质系统的多维互相关弛豫法

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摘要

We report, for the first time, the application of multidimensional cross-correlation relaxometry to a model globular aqueous protein system (bovine serum albumin) over a wide range of water contents from the solution to glassy states. Off-diagonal cross-relaxation peaks are observed and lend support to the proton-exchange cross-relaxation model of water relaxation. The dependence of the water proton relaxation rates on water content is also consistent with the multistate theory of water dynamics in protein systems. Evidence for water compartmentation in bovine serum albumin gels is presented and the potential of multidimensional cross-correlation nuclear magnetic resonance relaxometry in elucidating water-biopolymer interactions in more complex heterogeneous biopolymer systems is discussed.
机译：我们首次报告了多维互相关弛豫法在从溶液状态到玻璃态的广泛水含量范围内对模型球状含水蛋白系统（牛血清白蛋白）的应用。观察到非对角交叉松弛峰，并为水松弛的质子交换交叉松弛模型提供支持。水质子弛豫速率对水含量的依赖性也与蛋白质系统中水动力学的多态理论一致。提出了在牛血清白蛋白凝胶中进行水区分开的证据，并讨论了多维互相关核磁共振弛豫法在阐明更复杂的异质生物聚合物系统中水与生物聚合物相互作用中的潜力。

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