Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.
Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.
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DOI：
10.1021/bi00124a006
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发表时间：
1993-07
期刊：
影响因子：
2.9
通讯作者：
R. F. Tilton;John C. Dewan;G. Petsko
中科院分区：
文献类型：
--
作者：
R. F. Tilton;John C. Dewan;G. Petsko
用1.5埃分辨率的X射线衍射数据测定了核糖核酸酶-A蛋白在98 - 320 K九个不同温度下的结构。它是确定的蛋白质分子膨胀轻微（0.4%每100 K）随着温度的升高，这种膨胀是线性的。这种扩张主要是由于分子的细微重新包装，暴露的和移动的环区域表现出最大的运动。单个原子的Debye-Waller因子主要表现为双相行为，在低温下具有较小的正斜率，在较高温度下具有较大的正斜率。该曲线中的断裂发生在180-200 K的特征温度处，这可能表明周围蛋白质溶剂的动力学结构发生了根本变化。随着温度的升高，蛋白质Debye-Waller因子的分布变宽，并向更高的值移动。
Structures using X-ray diffraction data collected to 1.5-A resolution have been determined for the protein ribonuclease-A at nine different temperatures ranging from 98 to 320 K. It is determined that the protein molecule expands slightly (0.4% per 100 K) with increasing temperature and that this expansion is linear. The expansion is due primarily to subtle repacking of the molecule, with exposed and mobile loop regions exhibiting the largest movements. Individual atomic Debye-Waller factors exhibit predominantly biphasic behavior, with a small positive slope at low temperatures and a larger positive slope at higher temperatures. The break in this curve occurs at a characteristic temperature of 180-200 K, perhaps indicative of fundamental changes in the dynamical structure of the surrounding protein solvent. The distribution of protein Debye-Waller factors is observed to broaden as well as shift to higher values as the temperature is increased.