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- W2000754306 abstract "We have applied atomic force microscopy (AFM) and single molecule force spectroscopy (SMFS) to characterize the structure and molecular mechanics of clathrin triskelia. The latter are the basic building blocks of the protein coat surrounding plasma-membrane-derived vesicles involved in receptor-mediated endocytosis. Here we resolve variable profiles of individual triskelia on mica surfaces for the first time by AFM, at a resolution comparable to that of electron microscopy. Classical three-leg, filamentous pin-wheel shapes, as well as dimers and non-planar triskelion conformations, are readily observed. Time sequences of AFM images clearly demonstrate conformation fluctuations in single triskelia when the latter are in physiological solutions. Additionally, AFM SMFS reveals, also for the first time, a series of internal energetic barriers that characterize triskelion heavy chain domain folding, corresponding to numerous alpha-helix hairpins of ca. 30 amino acid residues, and variable unfolding of larger, cooperative hairpin domains up to the size of the known repeating motif of ca. 145 amino acid residues. The dynamic domain rupture force ranges from a few 10s pN to over 500 pN, increasing continuously as the stretching loading rate changes over the range from 100 to 105 pN/s. The results once again show AFM to be a powerful tool for biomedical imaging and nanometric single molecule characterizations." @default.
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- W2000754306 date "2009-02-01" @default.
- W2000754306 modified "2023-10-05" @default.
- W2000754306 title "AFM Visualization and Force Spectroscopy of Clathrin Triskelia" @default.
- W2000754306 doi "https://doi.org/10.1016/j.bpj.2008.12.2018" @default.
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