Beatrix Ueberheide

Scientific Advisor at Protein Metrics

Dr. Ueberheide is the Director, Proteomics Resource Center, and Assistant Professor of Biochemistry and Molecular Pharmacology at New York University (NYU) Langone Medical Center.

As the Director of Proteomics she enables the NYU faculty in their research efforts to understand cellular function by characterizing proteins in a biological context. The current focus of her research is to develop advanced mass- spectrometry based techniques to characterize circulating antibodies and to understand the structure-function relationship of peptide toxins. She utilizes chemical strategies in combination with electron transfer dissociation to increase the biologically relevant information obtained from mass spectrometric data.

In her collaboration with Protein Metrics, Professor Ueberheide is using Protein Metrics’ Byonic™, Bylogic ®, Super Novo™, and Intact Mass™ to develop a variety of applications, including de novo sequencing, cross-ink analysis for Higher Order Structure, PTM analysis, and glyco analysis.

Dr. Ueberheide joined the faculty of NYU as the Director of the Proteomics Resource Center in 2011, establishing a fully integrated state of the art mass spectrometry laboratory focusing on proteomics. She has extensive experience in biological mass spectrometry especially method development, mapping of post translational modifications, de novo sequencing, Bottom Up and Top Down strategies, as well as comprehensive protein characterization in complex mixtures.

Dr. Ueberheide has contributed to a wide range of studies from analyzing chromatin, characterizing venoms, to sequencing of complex antibody mixtures.

She joined Rockefeller University in 2006 for her postdoctoral training. There she developed de novo sequencing strategies for analysis of venom components and established techniques to study antibodies isolated from HIV infected long-term non-progressors.

She received her Ph.D. in chemistry at the University of Virginia where she focused on the study of histone post translational modifications using classical Bottom Up and also Top Down strategies.


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