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The compression process of a single bovine carbonic anhydrase II ( BCA II ) molecule by an atomic force microscope (AFM) tip in ultra high vacuum (UHV) condition is studied by the molecular dynamics (MD) simulations with the all-atom empirical force field model. The temperature is assumed to be 0 and 300 K, and the force curves are calculated with both the tip and surface modeled as rigid planar graphite sheets. At T = 0 K the normal force of the tip increases gently after the tip starts to compress the protein molecule, as the external force by the tip is consumed to relax the turn or coil structures on the outer part of the protein. However, once this region is deformed to take a flat structure, the normal force increases rapidly. The general trend in the force curves at T = 300 K is similar to that observed at T = 0 K, although the relaxation inside the protein is promoted thermally to reduce the normal force observed. Furthermore, the saw-tooth peaks observed in the force curves are found to originate from the sudden collective sliding motion of the residues, which is triggered by the slip of the locally contacting turn or coil structures at the atomic level. [DOI: 10.1380/ejssnt.2006.552]

Discontinuous Force Compression Curve of Single Bovine Carbonic Anhydrase Molecule Originated from Atomistic Slip