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Titlebook: Atomic Force Microscopy; Methods and Protocol Nuno C. Santos,Filomena A. Carvalho Book 2019 Springer Science+Business Media, LLC, part of S

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樓主: Inveigle
21#
發(fā)表于 2025-3-25 05:45:38 | 只看該作者
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發(fā)表于 2025-3-25 07:58:48 | 只看該作者
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發(fā)表于 2025-3-25 12:53:15 | 只看該作者
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發(fā)表于 2025-3-25 16:40:18 | 只看該作者
https://doi.org/10.1007/978-3-319-26656-5 surface and the changes in the force required for membrane piercing upon incubation with this special type of proteins. Here we describe robust protocols to investigate the effect of pore-forming proteins in supported lipid bilayers.
25#
發(fā)表于 2025-3-25 20:26:32 | 只看該作者
Artifacts and Practical Issues in Atomic Force Microscopyn many cases, training in AFM is inadequate. In this chapter we show examples of common artifacts in AFM and describe, where possible, how to overcome them. Other practical issues important for best practice in AFM operation, such as noise reduction and data processing, are also discussed.
26#
發(fā)表于 2025-3-26 03:06:09 | 只看該作者
Imaging Artificial Membranes Using High-Speed Atomic Force MicroscopyIn this context, we have developed new protocols adapted for HS-AFM to form supported lipid bilayers on small mica disks using the vesicle fusion or Langmuir-Blodgett methods. In this chapter we describe in detail the protocols to fabricate supported artificial bilayers as well as the main guidelines for HS-AFM imaging of such samples.
27#
發(fā)表于 2025-3-26 06:59:25 | 只看該作者
28#
發(fā)表于 2025-3-26 11:05:51 | 只看該作者
Ligand-Receptor Binding on Cell Membrane: Dynamic Force Spectroscopy Applicationss, disease pathogenesis, and mechanism of drugs. Here we describe an example of applying single-molecule dynamic force spectroscopy to study the binding of epidermal growth factor (EGF) to its receptor EGFR, as well as the effect of two clinical drugs, Pertuzumab and Trastuzumab, on the interaction of EGF and EGFR.
29#
發(fā)表于 2025-3-26 15:56:52 | 只看該作者
30#
發(fā)表于 2025-3-26 20:04:29 | 只看該作者
https://doi.org/10.1007/978-3-7908-1835-2roteins. Herein, a method for analyzing a complex formed by a telomeric DNA sequence wrapped around the TRF2 binding protein is presented. The described procedure could be applied to the study of any type of DNA–protein complex.
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