通过寿命分辨荧光各向异性观察蛋白质中色氨酸残基的纳秒级片段迁移率。
Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies.
作者信息
Lakowicz J R, Freshwater G, Weber G
出版信息
Biophys J. 1980 Oct;32(1):591-601. doi: 10.1016/S0006-3495(80)84992-7.
Abstract
Steady-state and lifetime-resolved fluorescence anisotropy measurements of protein fluorescence were used to investigate the depolarizing motions of tryptophan residues in proteins. Lifetime resolution was achieved by oxygen quenching. The proteins investigated were carbonic anhydrase, carboxypeptidase A, alpha-chymotrypsin, trypsin, pepsin, and bovine and human serum albumin. When corrected for overall protein rotation, the steady state anisotropies indicate that, on the average, the tryptophan residues in these proteins rotate 29 degrees +/- 6 degrees during the unquenched excited state lifetimes of these proteins, which range from 1.7 to 6.1 ns. The lifetime-resolved anisotropies reveal correlation times for these displacements ranging from 1 to 12 ns. On the average these correlation times are tenfold shorter than that expected for overall protein rotation. We conclude that the tryptophan residues in these proteins display remarkable freedom of motion within the protein matrix, which implies that these matrices are highly flexible on the nanosecond time scale.
摘要
利用蛋白质荧光的稳态和寿命分辨荧光各向异性测量来研究蛋白质中色氨酸残基的去极化运动。通过氧猝灭实现寿命分辨。所研究的蛋白质有碳酸酐酶、羧肽酶A、α-胰凝乳蛋白酶、胰蛋白酶、胃蛋白酶以及牛血清白蛋白和人血清白蛋白。在对整体蛋白质旋转进行校正后，稳态各向异性表明，平均而言，这些蛋白质中的色氨酸残基在这些蛋白质未猝灭的激发态寿命期间旋转29度±6度，这些寿命范围为1.7至6.1纳秒。寿命分辨各向异性揭示了这些位移的相关时间范围为1至12纳秒。平均而言，这些相关时间比整体蛋白质旋转预期的时间短十倍。我们得出结论，这些蛋白质中的色氨酸残基在蛋白质基质内表现出显著的运动自由度，这意味着这些基质在纳秒时间尺度上具有高度的灵活性。
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