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• W2000667711 abstract "We use atomic force microscopy (AFM) based force-compression measurements to probe the ligand-induced functional conformational changes in surface-immobilized dicysteine-terminated maltose binding proteins (dicys-MBPs). The proteins are immobilized at well-defined locations directly on Au substrates using the previously reported technique of nanografting. By measuring the difference between the ligand-free and ligand-bound mechanical work performed by the AFM-tip during the protein compression, we determine the open−closed transition energy for dicys-MBPs to be ΔE0 = (8 ± 4) Kcal/mol. We also compare the binding kinetics of two different ligands (maltose and maltotriose) to dicys-MBPs by performing AFM-friction measurements. We show that our results are consistent with a simple model for the surface-immobilized dicys-MBPs: the protein consists of two rigid lateral lobes connected by a hinge-loaded spring." @default.
• W2000667711 created "2016-06-24" @default.
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• W2000667711 date "2008-07-22" @default.
• W2000667711 modified "2023-10-11" @default.
• W2000667711 title "Ligand-Induced Structural Changes in Maltose Binding Proteins Measured by Atomic Force Microscopy" @default.
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• W2000667711 doi "https://doi.org/10.1021/nl801553h" @default.
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