Jakob Ulmschneider 特别研究员
杰出人才类别: 
获得年份: 
2012
交叉科学研究所
Biophysics
包图 522
86-21-54743022
jakob@sjtu.edu.cn
1.Computational Biophysics, algorithmic development 2. Predicting the folding and native structure of membrane proteins 3. Design of auto-inserting, antimicrobial and cell-penetrating peptides

Professor Jakob Ulmschneider received his Ph.D. in Physics in 2004 from Yale University. He was an Emmy Noether Fellow at the Chemistry Department at the University of Rome ‘La sapienza’, Italy from 2005 to 2007, and a BIOMS Research Fellow at IWR at the University of Heidelberg from 2008 to 2011. In September 2011, he joined Institute of Natural Sciences at Shanghai Jiao Tong University and in 2012 was recipient of a Young 1000 Talent plan grant by the Chinese Government. His principle research interests include the study of membrane active peptides, computational structure prediction and simulation of membrane protein folding and function, and the study of voltage gated sodium channels.

  1. Wang, Y., Chen, C., Hu, D., Ulmschneider, M. , Ulmschneider, J.  Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide,  Nature Communications, 2016, 7, 13535.
  2. M. B. Ulmschneider, J. P. Ulmschneider, N. Schiller, B.A. Wallace, G. von Heijne & S. H. White.  Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion,  Nature Communications 2014, 5:4863
  3. R. McNulty, J. P. Ulmschneider, H. Luecke, M. B. Ulmschneider  Mechanisms of molecular transport through the urea channel of Helicobacter pylori , Nature Communications 2013, 4, 2900
  4. M.B. Ulmschneider, C. Bagnéris, E.C. McCusker, P. DeCaen, M. Delling, D.E. Clapham, J.P. Ulmschneider*, B. A. Wallace (*corresponding), Molecular Dynamics of Ion Transport through the Open Conformation of a Bacterial Voltage-gated Sodium Channel,Proc. Nat. Acad. Sci. 2013, 110, 6364
  5. J.P. Ulmschneider, J.C. Smith, S. H. White, M. B. Ulmschneider, In Silico Partitioning and Transmembrane Insertion of Hydrophobic Peptides Under Equilibrium Conditions, J. Am. Chem. Soc. 2011, 133, 15487-15495

     

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