COMPRESSIBILITY STRUCTURE RELATIONSHIP OF GLOBULAR-PROTEINS
COMPRESSIBILITY STRUCTURE RELATIONSHIP OF GLOBULAR-PROTEINS
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DOI：
10.1021/bi00369a034
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发表时间：
1986-10-21
期刊：
影响因子：
2.9
通讯作者：
HASEGAWA, Y
中科院分区：
文献类型：
--
作者：
GEKKO, K;HASEGAWA, Y
绝热压缩系数，. hivin.通过在25 ℃下的声速测量来测定水中11种球状蛋白质的β s。除枯草杆菌蛋白酶外，所研究的所有蛋白质均显示出正的β s值，表明蛋白质分子的大的内部可压缩性。蛋白质的固有压缩性的水化效果似乎是正常的冰。25种蛋白质的可压缩性数据，包括先前报道的14种[Gekko，K.，和Noguchi，H.（1979）J.Phys.Chem.83，2706-2714]进行统计分析，以检查压缩性与蛋白质的一些结构参数和氨基酸组成的相关性。结果发现，. hivin..β s随着蛋白质的部分比容和疏水性的增加而增加。螺旋元件似乎也是一个动态域，以增加. hivin.β s四个氨基酸残基（Leu，Glu，Phe和His）大大增加。另外四种（Asn、Gly、Ser和Thr）使其降低。基于未知蛋白质的氨基酸组成，计算未知蛋白质的β s值。由可压缩性数据揭示的蛋白质的体积波动在30-200 mL/mol的范围内，其对应于总蛋白质体积的约0.3%。构象波动似乎增强了蛋白质的热稳定性。
The adiabatic compressibility, .hivin..beta.s, of 11 globular proteins in water was determined by means of sound velocity measurements at 25.degree.C. All the proteins studied except for subtilisin showed positive .BETA.s values, indicating the large internal compressibility of the protein molecules. The intrinsic compressibility of proteins free from the hydration effect appeared to be comparable to that of normal ice. The compressibility data for 25 proteins, including 14 reported previously [Gekko, K., and Noguchi, H. (1979) J. Phys. Chem. 83, 2706-2714], were statistically analyzed to examine the correlation of the compressibility with some structural parameters and the amino acid compositions of proteins. It was found that .hivin..beta.s increases with increasing partial specific volume and hydrophobicity of proteins. The helix element also seemed to be a dynamic domain to increase .hivin..beta.s. Four amino acid residues (Leu, Glu, Phe, and His) greatly increased .hivin..beta.s, and another four (Asn, Gly, Ser, and Thr) decreased it. Some empirical equations were derived for the estimation of the .hivin..beta.s values of unknown proteins on the basis of their amino acid compositions. The volume fluctuations of proteins revealed by the compressibility data were in the range of 30-200 mL/mol, which corresponded to about 0.3% of the total protein volume. The conformational fluctuation seemed to enhance the thermal stability of proteins.