Experimental and Modeling Study of the Optical Properties, Heat and Cold Tolerance, and UV-Resistance of the Eye Lens Crystallins

非技术性：该奖项由加州尔湾大学材料研究部生物材料项目颁发，旨在表彰对自然界如何产生透明、耐用的生物材料的科学理解，例如构成眼睛透镜的蛋白质。虽然这些蛋白质的分子细节在不同的生物体中有所不同，但它们在高稳定性和对极端温度和紫外线损伤的抵抗力方面功能相似。了解不同透镜蛋白质的共同结构因素将有助于指导未来耐温抗紫外仿生材料的设计。教育计划包括培养博士生。和本科水平。这些学生将接受培训，不仅在完成研究所需的具体技能，而且在跨学科界限的思维和解决问题。另一个重要组成部分是向初中和高中学生推广。推广计划的目标是增加中学生对科学作为职业的兴趣，包括各种活动和参观PI的实验室。技术支持：该项目旨在了解蛋白质稳定性的分子基础，特别是对极端温度和紫外线暴露的抵抗力。对不同源但发挥相同功能作用的极其稳定的结构蛋白的研究将提供对稳定性的序列决定因素的深入了解，而不受由于热稳定酶中的酶活性而保守的效应的干扰。为这项工作选择的特定蛋白质是来自三种适应极端环境的生物体的眼透镜晶体蛋白。 箱形水母（Tripedalia cystophora）J2-晶体蛋白具有很高的热稳定性，而来自南极洋枪鱼（Dissostichus mawsoni）的γ-S1-和γ-S2-晶体蛋白有助于赋予这种生物体的眼睛透镜不寻常的耐寒性。 昼行性壁虎Lygodactylus picturatus的iota-晶状体蛋白具有涉及视黄醇衍生物结合的不寻常的UV保护机制。核磁共振和光学光谱的研究加上分子动力学和蒙特卡罗模拟将阐明重要的结构因素和分子间的相互作用，赋予这些蛋白质的高稳定性，指导未来的仿生材料的设计。教育计划包括培养博士生。和本科水平，谁将接触到广泛的实验和计算技术，以及针对中学生的成功推广计划的延续。

Nontechnical: This award by the Biomaterials Program in the Division of Materials Research to University of California Irvine is for developing a scientific understanding of how nature produces transparent, durable biomaterials, as exemplified by the proteins making up the eye lens. Although the molecular details of these proteins vary among different organisms, they are functionally similar in their high stability and resistance to temperature extremes and UV-light damage. Understanding the structural factors diverse lens proteins have in common will help guide the design of future temperature and UV-resistant biomimetic materials. The educational plan includes training of students at the Ph.D. and undergraduate levels. These students will be trained not only in the specific skills needed to complete the research, but also in thinking and problem-solving across disciplinary boundaries. Another important component is outreach to middle school and high school students. The goal of the outreach program is to increase interest in science as a career among middle school students and includes a variety of activities and visits to the PI's labs. Technical: This project seeks to understand the molecular basis of protein stability, in particular resistance to extreme temperatures and UV light exposure. Studies of extremely stable structural proteins that are not homologous but play the same functional role will provide insight into sequence determinants of stability without interference from effects that are conserved due to enzymatic activity in thermostable enzymes. The particular proteins chosen for this effort are eye lens crystallins from three organisms adapted to extreme environments. The box jellyfish (Tripedalia cystophora) J2-crystallin has a high thermal stability, while the gamma-S1- and gamma-S2-crystallins from the Antarctic toothfish (Dissostichus mawsoni) help confer unusual cold tolerance on the eye lens of this organism. The iota-crystallin of the diurnal gecko Lygodactylus picturatus, has an unusual UV protection mechanism involving binding of a retinol derivative. NMR and optical spectroscopic studies coupled with molecular dynamics and Monte Carlo simulations will elucidate the important structural factors and intermolecular interactions that confer high stability on these proteins, guiding the future design of biomimetic materials. The educational plan includes training of students at the Ph.D. and undergraduate levels, who will be exposed to a broad range of experimental and computational techniques, as well as the continuation of a successful outreach program aimed at middle school students.