Atomic Force Microscopy - Investigns. Into Biology - From - download pdf or read online

By C. Frewin

ISBN-10: 9535101145

ISBN-13: 9789535101147

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Biophys. , Vol. 75, pp. 3008–3014. Schlierf, M. & Rief, M. (2005). Temperature softening of a protein in singlemolecule experiments. J Mol Biol, Vol. 354, pp. 497-503. Seo, Y. & Jhe, W. (2008). Atomic force microscopy and spectroscopy. REPORTS ON PROGRESS IN PHYSICS, Vol. 71, 016101, 24pp. Smith, S. ; Finzi, L. & Bustamante, C. (1992). Direct mechanical measurements of the elasticity of single DNA-molecules by using magnetic beads. Science, Vol. 258, pp. Wright, C. ; Shah, M. ; Powell, L. ; et al.

1 oscillations, which reduce the quality of the image, were clearly visible. 05, the oscillations were still visible, and features were distorted. a) topography image, b) phase image. 3 Artifacts related to the sample properties The next group of artifacts appears due to specific properties of a sample. For example, the sample can drift in one direction even if it is well attached to the sample holder. If this drift is due to thermal drift, one can reduce it by stabilizing the temperature. If it is due to other reasons, one can scan faster (Eaton, 2010).

2009). Surfaces with O-termination were highly resistive. The H-terminated diamond is a hydrophobic surface, contact angle ~ 80-100 °. The O-terminated diamond has hydrophilic properties, contact angle ~ 5-20 °. Proteins were adsorbed on the MCD substrates from 15 % fetal bovine serum (FBS) solution (PAA) in McCoy‘s 5A medium with stable Glutamine without Phenolred (BioConcept). The serum contains several proteins, usually bovine serum albumin, fibronectin and vitronectin. FBS is heat inactivated (56 °C, 25 min) to destroy the immunological components yet to preserve the proteins.

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Atomic Force Microscopy - Investigns. Into Biology - From Cell to Protein by C. Frewin

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