Molecular modeling of protein materials: case study of elastin
Molecular modeling of protein materials: case study of elastin
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DOI：
10.1088/0965-0393/21/6/063001
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发表时间：
2013-09
影响因子：
1.8
通讯作者：
A. Tarakanova;M. Buehler
中科院分区：
文献类型：
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作者：
A. Tarakanova;M. Buehler
蛋白质材料的分子建模是一个快速发展的研究领域，在结构工程、医学和生物学等领域做出了许多贡献。我们回顾了蛋白质材料分子模拟的历史和常用方法，强调了使用模拟作为实验工作的补充的优势。然后，我们考虑一个案例研究的蛋白质弹性蛋白，一个至关重要的“机械蛋白质”，在分子建模领域的方法，取得了显着的影响。我们概述了计算建模研究的进展，这些研究大大增强了我们对这种重要蛋白质的理解，这种蛋白质赋予了它所发现的组织的弹性和回弹力，包括皮肤，肺，动脉和心脏。半个多世纪以来，大量的文献都致力于研究这种蛋白质的结构和功能，第一个弹性蛋白的分子动力学研究是在20世纪80年代报道的。我们回顾了关键的计算工作，大大提高了我们的基本理解弹性蛋白的原子结构和其非凡的品质，特别是集中在两个：弹性蛋白的高超的弹性和逆温度转换的显着能力的弹性蛋白采取更结构化的构象在更高的温度，这表明其有效性作为生物分子开关。我们的希望是展示这些方法作为补充和丰富的实验方法，迄今为止，占主导地位的研究大多数蛋白质为基础的材料。
Molecular modeling of protein materials is a quickly growing area of research that has produced numerous contributions in fields ranging from structural engineering to medicine and biology. We review here the history and methods commonly employed in molecular modeling of protein materials, emphasizing the advantages for using modeling as a complement to experimental work. We then consider a case study of the protein elastin, a critically important ‘mechanical protein’ to exemplify the approach in an area where molecular modeling has made a significant impact. We outline the progression of computational modeling studies that have considerably enhanced our understanding of this important protein which endows elasticity and recoil to the tissues it is found in, including the skin, lungs, arteries and the heart. A vast collection of literature has been directed at studying the structure and function of this protein for over half a century, the first molecular dynamics study of elastin being reported in the 1980s. We review the pivotal computational works that have considerably enhanced our fundamental understanding of elastin's atomistic structure and its extraordinary qualities—focusing on two in particular: elastin's superb elasticity and the inverse temperature transition—the remarkable ability of elastin to take on a more structured conformation at higher temperatures, suggesting its effectiveness as a biomolecular switch. Our hope is to showcase these methods as both complementary and enriching to experimental approaches that have thus far dominated the study of most protein-based materials.