Emerging Researchers National (ERN) Conference

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A glimpse of structural biology research at an HBCU

Faculty #9
Discipline: Chemistry & Chemical Sciences
Subcategory: STEM Research

Steven Damo - Fisk University

Protein-protein interactions modulate a diverse array of critical biological responses from signal transduction to protection from oxidative stress. Structural biology is the method of choice for elucidating the atomic-resolution details of biological mechanisms. However, techniques such as x-ray crystallography and NMR spectroscopy require expensive instrumentation and are not readily accessible at primarily teaching institutions. Leveraging geographic proximity to research intensive institutions, an innovative Master’s to PhD Bridge Program, and a surplus of motivated undergraduates, Fisk University has initiated a strategic curriculum reform to emphasize the quantitative nature of biological data, including structural biology. A combination of computational and experimental biophysical approaches has been applied to understand the mechanism of ligand binding to the receptor for advanced glycation end products (RAGE) and the structural dynamics of superoxide dismutase. Protein docking strategies coupled with isothermal titration calorimetry experiments and dynamic light scattering have identified an essential charged surface of RAGE that recognizes S100 ligands. These studies represent important first steps toward characterizing the mechanism of RAGE activation, an essential component of inflammation. Additionally, the high resolution x-ray crystal structure of a bacterial manganese dependent superoxide dismutase has been determined and its thermal stability quantified using differential scanning calorimetry. These studies were initiated as part of an effort to embed authentic research in the physical chemistry course associated laboratory. Together, these research projects demonstrate the feasibility of conducting structural biology research at an HBCU.

Funder Acknowledgement(s): NSF 1547757; NSF 1400969; NSF 1623280

Faculty Advisor: None Listed,

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This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.