1995年7月辽宁师范大学获学士学位；2000年7月吉林大学获博士学位。2000年9月至2001年10月，在中科院大连化学物理研究所从事博士后研究工作。2001年11月至2005年5月，先后在美国Scripps研究所及德州大学休斯顿健康信息中心的Willy Wriggers研究组任博士后。其中2004年1月至2005年12月获美国W. M. Keck 基金会Postdoctoral Fellowship资助。2005年6月至2011年7月，美国Baylor College of Medicine，先后任Research Associate, Instructor。2011年7月起，任中科院上海生科院生化与细胞所研究员、博士生导师。获国家基金委“优秀青年”（2013年）基金资助。

本研究组致力于解析分子伴侣协助下的蛋白质折叠与解聚的机理。主要实验手段包括超低温冷冻电镜(cryo-EM)单颗粒重组以及低温电子断层扫描技术(cryo-Electron Tomography)，并结合生物信息学和分子柔性装配等计算工具。 蛋白质折叠中的缺陷通常伴随着许多人类疾病，包括癌症及蛋白聚集引起的神经退行性疾病，如帕金森氏综合症和亨廷顿舞蹈病等。分子伴侣(chaperone)是一类可以协助细胞中蛋白质正确折叠的分子机器，其中真核细胞中双环背对背堆叠的多聚体分子伴侣素(chaperonin)TRiC/CCT是最为复杂的分子伴侣。它可以帮助~5-10%胞质蛋白的折叠，包括许多重要的结构和调节蛋白。然而，由于其结构的复杂性导致对此重要分子机器的结构知之甚少。我们的研究兴趣在于解析分子伴侣如TRiC是如何识别并结合它的底物，三磷酸腺苷(ATP)触发下其构象变化与底物蛋白正确折叠之间的相互关系。长期着眼，我们会进一步研究重要分子伴侣极其cochaperone之间如何相互作用来共同协助底物蛋白质的折叠与解聚。 我们的另外一个研究方向是二维图像对位(image alignment)方法及分子柔性装配(flexible fitting)工具的发展及其在cryo－EM数据处理中的应用。我们发展了创新性的二维快速转动匹配方法，简称FRM2D。该方法不仅计算精度高于传统方法并且极大缩减了计算时间。此方法已成功应用于十余个中、高分辨率大分子复合物结构的三维重组过程中。此外，FRM2D方法已被嵌入冷冻电镜领域三大应用最广泛的单颗粒重组软件包之一EMAN之中，供其在世界范围内的用户免费使用

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