首页> 外文期刊>Physical review, E. Statistical physics, plasmas, fluids, and related interdisciplinary topics >Effects of ultraviolet radiation on the type-I collagen protein triple helical structure: A method for measuring structural changes through optical activity - art. no. 031920
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Effects of ultraviolet radiation on the type-I collagen protein triple helical structure: A method for measuring structural changes through optical activity - art. no. 031920

机译:紫外线对I型胶原蛋白三螺旋结构的影响:一种通过光学活性测量结构变化的方法-艺术。没有。 031920

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摘要

A detailed study of the effects of ultraviolet radiation on type-I collagen has been conducted. We have confirmed that exposure to ultraviolet radiation lowers the denaturation temperature of type-I collagen and that the triple helical state is destroyed provided that the radiation dose exceeds a threshold level, which is defined as the incident radiation dose that raises the sample temperature above the (lower) denaturation temperature. For incident radiation doses below threshold, the collagen molecule remains in a triple helical state. Denaturation is determined by changes in the optical activity of the collagen solution. Furthermore, a new instrument has been developed and tested to measure the optical rotatory dispersion properties of chiral molecules. The advantage of this instrument is that it enables a real-time measurement of the optical activity of chiral macromolecules while exposing samples to ultraviolet radiation and requiring no special sample preparation techniques. Using a differential measurement scheme, system errors have been minimized. [References: 33]
机译:已经进行了紫外线辐射对I型胶原蛋白影响的详细研究。我们已经确认,暴露于紫外线辐射会降低I型胶原蛋白的变性温度,并且只要辐射剂量超过阈值水平(定义为入射辐射剂量会使样品温度升高至高于260℃),三螺旋状态就会被破坏。 (降低)变性温度。对于低于阈值的入射辐射剂量,胶原分子保持三重螺旋状态。变性通过胶原溶液的光学活性的变化来确定。此外,已经开发并测试了新的仪器以测量手性分子的旋光性。该仪器的优势在于,它可以实时测量手性大分子的光学活性,同时将样品暴露于紫外线中,并且不需要特殊的样品制备技术。使用差分测量方案,可以将系统误差降至最低。 [参考:33]

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