IBBR Seminar Series
Amino acids comprise structures of various sizes, ranging from a short chain of a peptide to complex macromolecular assemblies. By modifying residues within peptides and proteins or proteins that make up the assemblies, we can gain insight into the modification target’s native function or enhance its function. In this talk, I will describe how I have successfully used protein engineering approaches to modify the properties of targets of different sizes, including an antimicrobial peptide (small), a fluorescent protein (medium), and a protein shell assembly (large).
Abstract: Recent advances at the intersection of nanofabrication and biotechnology exploit novel bionanomaterials to marry bottom-to-top self-assembly with top-down lithographic methods. In biotechnology, bionanomaterials include monoclonal antibodies as well as components of nanoscale drug delivery vectors. Structural measurements on bionanomaterials enable design and engineering of robust, reliable systems.
Lisa Kilpatrick (Bioanalytical Science Group): "Investigating Quantification Accuracy for Vitamin D-Binding Protein"
Robert Dejaco (Mathematical Analysis and Modeling Group): “Background Fluorescence in qPCR"
Meeting number: 120 273 5751
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Protein function can be progressively fine-tuned by substituting amino acids at “rheostat” positions. For example, at a rheostat position that modulates binding affinity, substitutions exhibit Kd values that span a wide range. Early studies of rheostat positions revealed outcomes that could not be explained by side chain chemical similarities or by evolutionary frequency. In ongoing efforts to catalog the prevalence of rheostat positions, we have identified them in proteins that evolved under different physical constraints: globular soluble, integral membrane, and intrinsically disorder
Motivated by interest in the complex glycan shield on the SARS-CoV-2 Spike protein, we have undertaken a program to develop mass spectral libraries to aid in its characterization. We first extended our existing library and software to represent complex glycopeptides and then discovered an effective way to represent the site-specific distributions of N-glycans on any protein, including the 22 sites of the Spike. The evolution, future and applications of this program will be discussed.