澳门新莆京9288app官网(中国)有限公司

 

盖锋(Feng Gai)

教授,博士生导师

研究方向:物理化学,生物物理,分子光谱

办公室:A626
办公室电话:010-62752665
电子信箱:fgai@pku.edu.cn
课题组网站:www.chem.pku.edu.cn/gailab

学术简历:

  • 2021.12 – 至今 北京大学讲席教授,北京大学澳门新莆京9288app官网
  • 2014.7 – 2021.10 Edmund J. and Louise W. Kahn Term Professor,宾夕法尼亚大学化学系
  • 1999.8 – 2021.10 助理教授,副教授,教授,宾夕法尼亚大学化学系
  • 1997.6 – 1999.7 博士后,洛斯阿拉莫斯国家实验室
  • 1994.10 – 1997.5 博士后,哈佛大学化学系
  • 1989.7 – 1994.9 博士,爱荷华州立大学化学系
  • 1986.8 – 1989.6 讲师,清华大学化学系
  • 1983.9 – 1986.6 硕士,北京大学化学系
  • 1979.9 – 1983.6 学士,北京大学化学系

研究领域及兴趣:

应用基于分子振动和电子跃迁的线性和非线性光谱技术在分子层面上研究生物大分子的折叠机理、结构、构象动力学、功能以及它们之间的关系。目前的研究方向包括:
  1. 发展基于非天然氨基酸的光谱探针;
  2. 发展基于能量或电子转移的分子尺;
  3. 研究各种环境条件对生物分子的折叠、聚集、反应、和动力学的影响;
  4. 用非天然氨基酸调控生物化学反应;
  5. 发展基于散射的多维振动光谱技术;
  6. 发展基于化学反应的成像技术。

荣誉

  • Bayer Endowed Chair, Bayer-PKU Center for Translational Research (2021)
  • Peking University Chair Professor (2021)
  • Molecular Science Frontier Lecture Professorship, Institute of Chemistry, CAS (2016)
  • American Chemical Society Philadelphia Section Award (2014)
  • Alumni Excellence Award, Department of Chemistry, Iowa State University (2014)
  • Edmund J. and Louise W. Kahn Term Professor of Chemistry, UPenn (2014)
  • Fellow of the American Association for the Advancement of Science (2012)
  • Fellow of the American Physical Society (2011)
  • National Science Foundation CAREER Award (2001)
  • Research Innovation Award, Research Corporation (2000)
  • Director’s Postdoctoral Fellowship, Los Alamos National Lab (1997)
  • Zaffarano Prize for Graduate Student Research, Iowa State University (1994)
  • Henry Gilman Fellowship, Department of Chemistry, Iowa State University (1993)
  • Phillips Fellowship, Department of Chemistry, Iowa State University (1992)

代表性论文:(Perspective and Review)

  1. Tryptophan as a template for development of visible fluorescent amino acids. A. Acharyya, W. K. Zhang, and F. Gai. J. Phys. Chem. B 2021 125, 5458–5465.
  2. Infrared and fluorescence assessment of protein dynamics: From folding to function. B. Ding, M. R. Hilaire, and F. Gai. J. Phys. Chem. B 2016 120, 5103−5113.
  3. Biomolecular crowding arising from small molecules, molecular constraints, surface packing, and nano-confinement.  M. R. Hilaire, R. M. Abaskharon, and F. Gai.  J. Phys. Chem. Lett. 2015 6, 2546−2553.
  4. Site-specific infrared probes of proteins.  J. Q. Ma, I. M. Pazos, W. K. Zhang, R. M. Culik, and F. Gai.  Annu. Rev. Phys. Chem. 2015 66, 357–77.
  5. Spectroscopic studies of protein folding:  Linear and nonlinear methods.  A. L. Serrano, M. M. Waegele, and F. Gai. Prot. Sci. 2012 21, 157-170.
  6. Site-specific spectroscopic reporters of the local electric field, hydration, structure, and dynamics of biomolecules.  M. M. Waegele, R. M. Culik, and F. Gai. J. Phys. Chem. Lett. 2011 2, 2598–2609.

 

其它论文可通过Google Scholar搜索 (User Name: Feng Gai)

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