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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >PRESSURE-INDUCED CHANGE IN PROTEINS STUDIED THROUGH CHEMICAL MODIFICATIONS
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PRESSURE-INDUCED CHANGE IN PROTEINS STUDIED THROUGH CHEMICAL MODIFICATIONS

机译:通过化学修饰研究蛋白质引起的压力变化

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Pressure-induced change of two bovine proteins, or-lactalbumin (LA) and beta-lactoglobulin (LG), was investigated at neutral pH by means of fluorescence and CD spectroscopy. The rate and the extent of modification was considerably increased by applying high pressure during the dansylation reaction of LG, while those for LA were only moderately affected. This difference was accounted for by the structural deformation of these proteins under high pressure. The fluorescence spectrum of these proteins measured under elevated pressure, as well as their fluorescence and CD spectra after the pressure release, indicated different responses towards pressure. The structural change of LA was practically reversible up to 400 MPa, whereas that of LG lost reversibility at 150 MPa or lower. Fluorescent measurement of dansylated (prepared at atmospheric pressure) proteins, especially the energy transfer from the intrinsic Trp residue to the dansyl group, showed that the protein structure was deformed by pressure and that the energy transfer facility of the two proteins was differently affected by high pressure, probably reflecting the degree of compactness of their pressure-perturbed structures. [References: 34]
机译:在中性pH下,通过荧光和CD光谱研究了压力诱导的两种牛蛋白或乳白蛋白(LA)和β-乳球蛋白(LG)的变化。通过在LG的丹磺酰化反应过程中施加高压可以显着提高修饰的速率和程度,而对于LA的修饰作用则只有中等程度的影响。这些差异是由于这些蛋白质在高压下的结构变形造成的。这些蛋白质在高压下测得的荧光光谱,以及在释放压力后的荧光和CD光谱,表明对压力的响应不同。 LA的结构变化在最高400 MPa时实际上是可逆的,而LG的结构变化在150 MPa或更低时丧失了可逆性。荧光检测丹磺酰化(在大气压下制备)的蛋白质,特别是从固有Trp残基到丹磺酰基的能量转移,结果表明蛋白质结构在压力作用下发生了变形,并且两种蛋白质的能量转移设施受高压的影响不同。压力,可能反映了其受压结构的紧凑程度。 [参考:34]

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