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De Novo Design of a βαβ Motif
Authors:Huanhuan Liang  Hao Chen Dr  Keqiang Fan Dr  Ping Wei Dr  Xianrong Guo Dr  Changwen Jin Prof  Chen Zeng Prof  Chao Tang Prof  Luhua Lai Prof
Institution:1. College of Chemistry and Molecular Engineering, Peking University, Beijing 100871 (China);2. Department of Physics, The George Washington University, Washington, DC 20052 (USA);3. Beijing Nuclear Magnetic Resonance Center, Beijing 100871 (China);4. Departments of Biopharmaceutical Sciences and Biochemistry and Biophysics, University of California, San Francisco, CA 94158 (USA);5. State Key Laboratory for Structural Chemistry of Unstable and Stable Species, BNLMS, College of Chemistry and Molecular Engineering and Center for Theoretical Biology, Peking University, Beijing 100871 (China), Fax: (+86)?10‐6275‐1725, http://mdl.ipc.pku.edu.cn
Abstract:A designer monomeric protein with a βαβ fold—two parallel β strands connected by an α helix (see structure)—was constructed solely from coded amino acids. The high thermal stability of the structure is due to a large extent to tryptophan–tryptophan interactions between the two β strands.
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Keywords:foldamers  peptides  protein design  tertiary structure  WW interactions
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