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Computing the Fundamental Interactions Between Carbon Nanotubes and Pulmonary Surfactant Proteins

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dc.contributor.author Dharmadhikari, Bhushan V.
dc.date.accessioned 2015-09-09T13:45:55Z
dc.date.available 2015-09-09T13:45:55Z
dc.date.issued 2015-04
dc.identifier.citation B.V. Dharmadhikari, "Computing the Fundamental Interactions Between Carbon Nanotubes and Pulmonary Surfactant Proteins", Ph.D. dissertation, Dept. of Computer Science and Engineering, Univ. of Bridgeport, Bridgeport, CT, 2015. en_US
dc.identifier.uri https://scholarworks.bridgeport.edu/xmlui/handle/123456789/1314
dc.description.abstract Molecular dynamic computation is one of the most direct and detailed approaches for investigating protein and carbon nanotube interaction at the atomic level. Molecular dynamic computation can address the events occurring in a protein’s structure and on the surface of the carbon nanotube. Molecular dynamic computation can also explain the structural changes in protein, including (i) secondary and tertiary structure changes, (ii) orientation and reorientation of the protein before and after adsorption, (iii) behavior of each amino acid residual group, (iv) hydrogen-bonding, (v) pi-pi stacking of carbon atoms of proteins and carbon nanotube, and other things as well. These fundamental properties have to address the adsorption of protein on a carbon nanotube surface, and estimates of this process are produced by molecular dynamic computations. Also, molecular dynamic computation is an attractive method for 3D imaging in bio-nanotechnology because it can give a complete trajectory over time (tens or hundreds of nanoseconds) of all atoms of protein interacting with carbon nanotubes and thus clarify their behavior in a given environment. This work presents the fundamental understanding of the human pulmonary surfactant proteins SP-A, SP-B, SP-C, and SP-D and their interaction with a single-walled carbon nanotube. This is accomplished using nanoscale molecular dynamic computation. Atomistic molecular dynamic simulation is performed and a trajectory over 100 ns is computed. Results show that all four pulmonary surfactant proteins are adsorbed on the surface of a carbon nanotube. The main driving force of interaction is the Van der Waals force of attraction. From the root mean square deviation of all four protein trajectories, stability is achieved. Both hydrophobic and hydrophilic residues of proteins are adsorbed on the surface of a carbon nanotube. These results will be helpful in developing nano-electro-chemical biosensors in the future. en_US
dc.language.iso en_US en_US
dc.subject Computer engineering en_US
dc.subject Computer science en_US
dc.subject Carbon nanotube en_US
dc.subject Molecular dynamics simulation en_US
dc.subject Protein adsorption en_US
dc.subject Pulmonary surfactant proteins en_US
dc.title Computing the Fundamental Interactions Between Carbon Nanotubes and Pulmonary Surfactant Proteins en_US
dc.type Thesis en_US
dc.institute.department School of Engineering en_US
dc.institute.name University of Bridgeport en_US


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