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Chirality Based Separation of Carbon-Nanotubes by Analyzing the Specific Interaction with the AMB-1 Flagellin Derived Tri-Peptide.

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dc.contributor.author Singh, Shrishti
dc.contributor.author Macwan, Isaac
dc.contributor.author Patra, Prabir
dc.date.accessioned 2016-05-20T18:29:52Z
dc.date.available 2016-05-20T18:29:52Z
dc.date.issued 2016-04-28
dc.identifier.uri https://scholarworks.bridgeport.edu/xmlui/handle/123456789/1615
dc.description.abstract Isaac et. al (2015) studied the interaction between the flagellum of AMB-1 and different chirality CNTs (m-CNT and s-CNT). The observations through Molecular Dynamics simulations demonstrated that the glycine residues in D3 domain of flagellum interacts with m-CNT whereas such an interaction with s-CNT is absent. The specific interaction of glycine with m-CNT can lead to the development of a biological method for chirality based CNT sorting. Hence, further studies were required to determine the effect of the residues flanking glycine on it’s interaction with m-CNT. The type of interactions and the extent of interaction of different combinations of polar and non-polar amino acid residues flanking glycine were conducted. Hence, the role of glycine with two flanking amino acid residues (tripeptide) is substantiated to determine it’s specific interaction with m-CNT through the study of interaction energy and RMSD of the middle glycine and the flanking residues towards the adsorption of the tripeptide onto m-CNT. en_US
dc.language.iso en_US en_US
dc.publisher ASEE
dc.subject Carbon nanotube en_US
dc.subject AMB-1 en_US
dc.subject Tripeptide en_US
dc.title Chirality Based Separation of Carbon-Nanotubes by Analyzing the Specific Interaction with the AMB-1 Flagellin Derived Tri-Peptide. en_US
dc.type Presentation en_US
dc.institute.department School of Engineering en_US
dc.institute.name University of Bridgeport en_US
dc.event.location Kingston, RI en_US
dc.event.name 2016 ASEE Northeast Section Conference en_US


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