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Protein dynamics by the combination of high-speed AFM and computational modeling
Institution:1. Faculty of Pharmacy, Universiti Teknologi MARA Selangor, Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia;2. Collaborative Drug Discovery Research, Faculty of Pharmacy, Universiti Teknologi MARA Selangor, Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia;1. Magnetic Resonance Center (CERM), University of Florence, Via Sacconi 6, Sesto Fiorentino, 50019, Italy;2. Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, 50019, Italy;3. Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (CIRMMP), Via Sacconi 6, Sesto Fiorentino, 50019, Italy;1. Molecular Medicine Program, The Hospital for Sick Children, M5G 0A4, Toronto, Canada;2. Department of Biochemistry, The University of Toronto, M5G 1L7, Toronto, Canada;3. Department of Medical Biophysics, The University of Toronto, M5S 1A8, Toronto, Canada;1. State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;2. School of Life Sciences, Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong, China;1. Technische Universität Berlin, Chair of Bioanalytics, 10623 Berlin, Germany;2. Si-M/“Der Simulierte Mensch”, a Science Framework of Technische Universität Berlin and Charité - Universitätsmedizin Berlin, 10623 Berlin, Germany;3. Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, UK
Abstract:High-speed atomic force microscopy (HS-AFM) allows direct observation of biological molecules in dynamic action. However, HS-AFM has no atomic resolution. This article reviews recent progress of computational methods to infer high-resolution information, including the construction of 3D atomistic structures, from experimentally acquired resolution-limited HS-AFM images.
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