Descript |
349 p |
Note |
Source: Dissertation Abstracts International, Volume: 69-10, Section: B, page: 6125 |
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Adviser: George M. Whitesides |
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Thesis (Ph.D.)--Harvard University, 2008 |
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This dissertation describes the electrostatic self-assembly of charged, meso-scale components (objects having dimensions on the order of millimeters) into ordered two-dimensional (2D) structures. Meso-scale components are easy to fabricate, manipulate by hand, and visualize by eye. Systems of meso-scale components embody some aspects of molecular systems (e.g., electrostatic interactions), and therefore serve as simple, physical models that provide qualitative insight about molecular systems that assemble (Appendices III--VIII) |
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Electrostatic self-assembly is the process by which electrets---materials with a permanent electric field at their surface---form ordered structures. Charged, monopolar spheres (Chapter 2) and dipolar particles (Chapter 3) form 2D Coulombic crystals, which separate from uncharged, polarizable particles. These systems model the nucleation of crystals of polar molecules in a polarizable solvent. Appendix I describes the assembly of charged spheres that are threaded on a string---a system designed to model the folding of polymers. The materials in each of these studies charge by contact electrification (Appendix II), the process by which materials transfer charge when their surfaces contact each other |
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Self-assembled monolayers (SAMs) comprise a single layer of molecules that bind (covalently or non-covalently) to surfaces. SAMs can modify the chemical properties of surfaces and they may prove useful for incorporation into molecular electronic devices. The roughness of the surface affects the structure and electrical characteristics of the SAM. Part II of this dissertation describes the formation (Appendix III) and the structural and electrical characterization (Appendix IV) of well-ordered SAMs on ultraflat (template-stripped) surfaces |
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Appendices V--VIII describe the binding and self-assembly of proteins with small molecules (ligands and haptens). Appendix V reviews extensively the binding of monovalent and multivalent ligands to Carbonic Anhydrase. The binding of bivalent haptens to a monoclonal IgG antibody causes the antibody to form clusters that contain two or three antibody molecules (Appendix VII). This work is useful for purifying bivalent antibodies from a complex mixture of proteins (Appendix VI). Charged proteins can be---in some sense---classified as electrets; the acetylation of alpha-amylase produces highly negatively charged variants of the enzyme that resist aggregation and inactivation by anionic surfactants (Appendix VIII) |
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School code: 0084 |
Host Item |
Dissertation Abstracts International 69-10B
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Subject |
Chemistry, Physical
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Physics, Electricity and Magnetism
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Biophysics, General
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0494
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0607
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0786
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Alt Author |
Harvard University
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