Title:
Peptide and Protein Nanomaterials: The Design Challenge
Peptide and Protein Nanomaterials: The Design Challenge
dc.contributor.author | Conticello, Vincent | |
dc.contributor.corporatename | Georgia Institute of Technology. Institute for Electronics and Nanotechnology | en_US |
dc.contributor.corporatename | Emory University. Dept. of Chemistry | en_US |
dc.date.accessioned | 2015-11-13T20:59:18Z | |
dc.date.available | 2015-11-13T20:59:18Z | |
dc.date.issued | 2015-11-10 | |
dc.description | Presented at the Nano@Tech Meeting on November 10, 2015 at 12 noon in the Pettit Microelectronics Building Conference Room 102 A&B, Georgia Tech. | en_US |
dc.description | Vincent P. Conticello is a Professor in the Department of Chemistry at Emory University. His research interests lie in the design, synthesis, and characterization of synthetic materials derived from self-assembly of sequence-specific proteins and peptides. Vincent received his Ph.D. degree in Chemistry from Northwestern University under the direction of Professor Tobin Marks. He completed post-doctoral fellowships in Chemistry at Caltech (under Professor Robert Grubbs) and in Polymer Science at UMass-Amherst (under Professor David Tirrell). He joined Emory University as an Assistant Professor in 1995. | |
dc.description | Runtime: 58:15 minutes | |
dc.description.abstract | Structurally defined materials on the nanometer length-scale have been historically the most challenging to rationally construct and the most difficult to structurally analyze. Sequence-specific biomolecules, i.e., proteins and nucleic acids, have advantages as design elements for construction of these types of nano-scale materials in that correlations can be drawn between sequence and higher order structure, potentially affording ordered assemblies in which functional properties can be controlled through the progression of structural hierarchy encoded at the molecular level. However, the predictable design of self-assembled structures requires precise structural control of the interfaces between peptide subunits (protomers). In contrast to the robustness of protein tertiary structure, quaternary structure has been postulated to be labile with respect to mutagenesis of residues located at the protein-protein interface. We have employed simple self-assembling peptide systems to interrogate the concept of designability of interfaces within the structural context of nanotubes and nanosheets (see below). These peptide systems provide a framework for understanding how minor sequence changes in evolution can translate into very large changes in supramolecular structure, which provides significant evidence that the designability of protein interfaces is a critical consideration for control of supramolecular structure in self-assembling systems. | en_US |
dc.embargo.terms | null | en_US |
dc.format.extent | 58:15 minutes | |
dc.identifier.uri | http://hdl.handle.net/1853/54171 | |
dc.language.iso | en_US | en_US |
dc.publisher | Georgia Institute of Technology | en_US |
dc.relation.ispartofseries | Nano@Tech Lecture Series | |
dc.subject | Nanomaterials | en_US |
dc.subject | Nanotechnology | en_US |
dc.subject | Peptide | en_US |
dc.title | Peptide and Protein Nanomaterials: The Design Challenge | en_US |
dc.type | Moving Image | |
dc.type.genre | Lecture | |
dspace.entity.type | Publication | |
local.contributor.corporatename | Institute for Electronics and Nanotechnology (IEN) | |
local.relation.ispartofseries | Nano@Tech Lecture Series | |
relation.isOrgUnitOfPublication | 5d316582-08fe-42e1-82e3-9f3b79dd6dae | |
relation.isSeriesOfPublication | accfbba8-246e-4389-8087-f838de8956cf |
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