Show simple item record

dc.contributor.authorNakahara, Miwako
dc.date.accessioned2004-12-15T17:26:56Z
dc.date.available2004-12-15T17:26:56Z
dc.date.issued2004-12-15T17:26:56Z
dc.identifier.otherbibid: 6475968
dc.identifier.urihttps://hdl.handle.net/1813/227
dc.description.abstractThe characteristics of protein recognition and actuation on a silicon device are investigated using Dynamic Monte Carlo simulations with both a simple cubic lattice model and a high-resolution lattice model. The surface of a model device has a nanoscale electrostatic charge distribution produced by charged nanocrystals embedded into the model device. Thermodynamic and structural quantities of the protein-surface interaction are calculated using the Miyazawa-Jernigan contact energies for the simple cubic lattice model, and the Skolnick-Kolinski interaction scheme for the high-resolution lattice model. A parallel tempering method is applied in the simulation. The results indicate that the B1 domain of Protein G (1gb1) and two mutants of 1gb1s with the same mass, isoelectric points, and amino acids can be separated on the surface based on binding affinity differences. The differences are caused by the different surface charge distributions of the proteins. A protein with a more disperse charge distribution along the sequence has a lower affinity, while a protein with a more segregated charge distribution has a higher affinity. The segregated charge allows the protein to be denatured further by the generation of stronger Coulombic forces between the protein and the charged nanocrystals. This suggests that charge-patterned surfaces may be able to differentiate similar proteins that are usually difficult to separate by conventional methods. It is also demonstrated by the simulation that proteins can be actuated by switching and moving the charges of the nanocrystals. This result suggests that if fast reprogrammability of charges is realized, the device could be used to actuate a single biomolecular in a controllable manner. The simple cubic lattice model allows us to predict thermodynamic properties with ease, while the high-resolution lattice model enables us to estimate realistic protein structures. A combination of the two methods will be a useful tool to obtain thermodynamic, kinetic, and structural characteristics of protein adsorption on model devices.en_US
dc.format.extent1304007 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.subjectproteinen_US
dc.subjectsimulationen_US
dc.subjectMonte Carloen_US
dc.subjectnanocrystalen_US
dc.subjectsemiconductoren_US
dc.subjectmutanten_US
dc.subjectseparationen_US
dc.titleSIMULATION OF THE INTERACTION BETWEEN PROTEINS AND A CHARGE-NANOPARTTERNED SURFACEen_US
dc.typedissertation or thesisen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Statistics