Paper
19 November 2001 Simulation of the force-distance curves of atomic force microscopy for proteins by the Connolly surface approach
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Proceedings Volume 4590, BioMEMS and Smart Nanostructures; (2001) https://doi.org/10.1117/12.454603
Event: International Symposium on Microelectronics and MEMS, 2001, Adelaide, Australia
Abstract
An attempt to simulate the interaction between an AFM tip and a protein surface by employing the concept of Connolly molecular surface with a carbon probe has been investigated. A methodology has been developed to permit the computation of the Connolly surface for a protein, where numerous atoms are simultaneously interacting each other. The van der Waals and electrostatic interactions between the probe and the relevant Connolly surface elements are integrated to obtain the total interaction, resulting in a precise theoretical account for a variety of interaction components. The simulation offers a meaningful opportunity for AFM scientists to interpret AFM surface mapping results more precisely or on a more general level the polymer surface-protein surface interactions.
© (2001) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Jinan Cao, Duy K. Pham, Livia Tonge, and Dan V. Nicolau "Simulation of the force-distance curves of atomic force microscopy for proteins by the Connolly surface approach", Proc. SPIE 4590, BioMEMS and Smart Nanostructures, (19 November 2001); https://doi.org/10.1117/12.454603
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Cited by 2 scholarly publications.
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KEYWORDS
Proteins

Atomic force microscopy

Chemical species

Computer simulations

Chemistry

Carbon

Polymers

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