Goossens K, Smeller L, Frank J, Heremans K
Department of Chemistry, Katholieke Universiteit Leuven, Belgium.
Eur J Biochem. 1996 Feb 15;236(1):254-62. doi: 10.1111/j.1432-1033.1996.00254.x.
A hydrostatic pressure of 1.5 GPa induces changes in the secondary structure of bovine pancreatic trypsin inhibitor (BPTI) as revealed by the analysis of the amide I' band with Fourier-transform infrared (FTIR) spectroscopy in the diamond anvil cell. The features of the secondary structure remain distinct at high pressure suggesting that the protein does not unfold. The fitted percentages of the secondary structure elements during compression and decompression strongly suggest that the pressure-induced changes are reversible. The pressure-induced changes in the tyrosine side chain band are also reversible. The results demonstrate that the infrared technique explores different aspects of the behaviour of proteins in comparison with two published molecular dynamics studies performed up to 1 GPa [Kitchen, D.B., Reed, L.H. & Levy, R.M.(1992) Biochemistry 31, 10083-10093] and 500 MPa [Brunne, R.M. & van Gunsteren, W.F.(1993) FEBS Lett. 323, 215-217]. A possible explanation for the difference is the time scale of the experiments.
在金刚石对顶砧池中，通过傅里叶变换红外（FTIR）光谱对酰胺I'带进行分析发现，1.5吉帕的静水压力会引起牛胰蛋白酶抑制剂（BPTI）二级结构的变化。在高压下，二级结构的特征仍然明显，这表明蛋白质并未展开。压缩和减压过程中二级结构元素的拟合百分比有力地表明，压力诱导的变化是可逆的。酪氨酸侧链带的压力诱导变化也是可逆的。结果表明，与两项已发表的分别进行到1吉帕[Kitchen, D.B., Reed, L.H. & Levy, R.M.(1992) Biochemistry 31, 10083 - 10093]和500兆帕[Brunne, R.M. & van Gunsteren, W.F.(1993) FEBS Lett. 323, 215 - 217]的分子动力学研究相比，红外技术探索了蛋白质行为的不同方面。这种差异的一个可能解释是实验的时间尺度。
