Andrea G. Carter
- Courses5
- Reviews40
- School: East Carolina University
- Campus:
- Department: Chemistry
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Location:
E 5th St
Greenville, NC - 27858 - Dates at East Carolina University: November 2011 - July 2015
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Biography
East Carolina University - Chemistry
Assistant Professor of Chemistry | Meredith College
Higher Education
Andrea
Carter
Raleigh, North Carolina
Experienced and passionate chemistry educator with a background in biophysical chemistry. Past and/or present teacher of general chemistry, biochemistry, and physical chemistry with a particular interest in teaching scientific communication genres. Research interests include using guided inquiry in physical chemistry and investigating protein interactions.
Experience
East Carolina University
Teaching Assistant Professor of Chemistry
Andrea worked at East Carolina University as a Teaching Assistant Professor of Chemistry
East Carolina University
Teaching Instructor in Chemistry
Andrea worked at East Carolina University as a Teaching Instructor in Chemistry
Meredith College
Assistant Professor of Chemistry
Andrea worked at Meredith College as a Assistant Professor of Chemistry
Education
The Johns Hopkins University
Doctor of Philosophy - PhD
Program in Molecular Biophysics
North Carolina State University
Bachelor of Science - BS
Chemistry
North Carolina State University
Bachelor of Science - BS
Chemical Engineering with Biosciences Concentration
Park Scholar
https://park.ncsu.edu/
Publications
Mapping the Deltex-binding surface on the notch ankyrin domain using analytical ultracentrifugation.
Journal of Molecular Biology
The Notch signal transduction pathway controls cell fate determination during metazoan development. The Notch gene encodes a transmembrane receptor that is cleaved upon activation, liberating the Notch intracellular domain, which enters the nucleus and assembles transcriptional activation complexes that drive expression of Notch-responsive genes. The most conserved region of the Notch intracellular domain is an ankyrin domain (Nank), which binds directly to the cytosolic effector protein Deltex (Dx), controlling intracellular Notch activity. However, the structural and energetic basis for this interaction remains unknown. Here, we analyze the thermodynamics and hydrodynamics of the Nank:Dx heteroassociation, as well as a weaker Nank self-association, using sedimentation velocity analytical ultracentrifugation. By comparing g(s*) and c(s) distributions, and by direct fitting of sedimentation boundaries with thermodynamic association models, we were able to characterize the Nank:Dx heterodimer, measure its affinity, and map the interaction on the surface on Nank. N- and C-terminal deletions of whole ankyrin units implicate repeats 3 and 4 as key for mediating heteroassociation. An alanine scan across the interaction loops of Nank identifies a conserved hot spot in repeats 3 and 4, centered at R127, as critical for Dx binding. In addition, we were able to detect weak but reproducible Nank homodimerization (K(d) in the millimolar range). This association is disrupted by substitution of a conserved arginine (R107) with alanine, a residue previously implicated in a functionally relevant mode of interaction within dimeric transcription complexes. The distinct binding surfaces on Nank for homotypic versus Dx interaction appear to be compatible with teterameric Notch(2):Dx(2) assembly.
