Major
Biology
Anticipated Graduation Year
2025
Access Type
Restricted Access
Abstract
Binding affinity and binding specificity are two separate dimensions of molecular recognition. The former describes the affinity for the cognate ligand, while the latter describes the relative affinity of cognate to noncognate ligands. The experimental determination of affinity is straightforward, but it is much more difficult to measure specificity since it requires the characterization of “off-target” binding to any of a large number of potential noncognate ligands. The goal of my research project is to use a new approach, immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC/MS), to characterize the specificity of antibodies for their respective antigen as a function of their affinity maturation.
Faculty Mentors & Instructors
Dr. Joerg Zimmermann, Department of Chemistry and Biochemistry; Dr. Paul Chiarelli, Department of Chemistry and Biochemistry
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
USING IMMUNOPRECIPITATION-MASS SPECTROMETRY TO CHARACTERIZE CHANGES IN SPECIFICITY DURING ANTIBODY AFFINITY MATURATION
Binding affinity and binding specificity are two separate dimensions of molecular recognition. The former describes the affinity for the cognate ligand, while the latter describes the relative affinity of cognate to noncognate ligands. The experimental determination of affinity is straightforward, but it is much more difficult to measure specificity since it requires the characterization of “off-target” binding to any of a large number of potential noncognate ligands. The goal of my research project is to use a new approach, immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC/MS), to characterize the specificity of antibodies for their respective antigen as a function of their affinity maturation.