Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior.
Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior.
复制标题
人类 α-乳清蛋白的熔球:内部的水合、密度和可压缩性。
DOI:
10.1021/bi960264r
复制
发表时间:
1997
期刊:
影响因子:
2.9
通讯作者:
V. Bychkova
中科院分区:
文献类型:
--
作者:
D. P. Kharakoz;V. Bychkova
Specific partial volume, partial compressibility, and sound absorption changes induced by the native-to-molten globule state (acid) transition of the human alpha-lactalbumin were measured by means of densitometric and ultrasonic techniques and interpreted in terms of the protein molecule phase transition and interphase water transfer. The molten globule is a highly hydrated state containing about 270 water molecules inside. Intrinsic mass density of the hydrated (swollen) interior of the protein molecule is 5% smaller and the intrinsic compressibility coefficient 2 times higher than those in the native molecule. The obtained intrinsic compressibility falls into the range of values characteristic of highly associated liquids. Water inside the molten globule interior occupies less volume and is less compressible than in solvent phase. The acoustic relaxation was found to increase indicating an appearance of pressure-dependent processes. The commonly used approach to the calculation of the volume fluctuations of protein molecules, based on the well-known relation between the volume fluctuations and compressibility, is of limited applicability to the highly hydrated molten globule state because a large, if not predominant, part of the fluctuations may be determined by the process of water exchange between the molten globule and bulk solvent.