Title:
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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