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首页> 外文期刊>Biochemistry >Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior.
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Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior.

机译：人α-乳白蛋白的熔融小球：内部的水合作用，密度和可压缩性。

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摘要

Specific partial volume, partial compressibility and sound absorption changes induced by the native-to-molten globule (acid) transition of human alpha-lactalbumin were measured by densitometric and ultrasonic techniques and interpreted in terms of the protein molecule phase transition and interphase water transfer. The molten globule was highly hydrated, containing approximately 270 water molecules. Intrinsic mass density of the hydrated (swollen) interior of the protein molecule was 5% smaller andthe intrinsic compressibility coefficient 2-fold higher than those in the native molecule. The obtained intrinsic compressibility was within the range of values characteristic of highly associated liquids. Water inside the molten globule interior occupied less volume and was less compressible than in the solvent phase. It is concluded that the calculation of volume fluctuations of protein molecules, based on the relation between the volume fluctuations and compressibility, is of limited use in the highly hydrated molten globule state because a large part of the fluctuations may be determined by the process of water exchange between the molten globule and bulk solvent.
机译：由人α-乳白蛋白的天然-熔融小球（酸）转变引起的比体积，部分可压缩性和吸声变化通过光密度法和超声技术进行了测量，并根据蛋白质分子相变和相间水转移进行了解释。熔融的小球高度水化，包含约270个水分子。蛋白质分子的水合（溶胀）内部的本征质量密度比天然分子小5％，固有压缩系数高2倍。所获得的固有压缩率在高度缔合液体的特征值范围内。与溶剂相相比，熔融小球内部的水所占体积较小，可压缩性较小。结论是，基于体积波动和可压缩性之间关系的蛋白质分子体积波动的计算在水合高度熔融的球状状态中使用有限，因为大部分波动可能由水的过程确定。熔融小球与本体溶剂之间的交换。

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