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Sam is a structural biophysicist and computational chemist with over ten years of research experience deciphering the structure-function relationships of proteins and nucleoprotein complexes. She earned her first doctoral degree in Chemistry in the lab of Stephen Valentine at West Virginia University, where she focused on characterizing the conformational heterogeneity of peptides and intrinsically disordered proteins (IDPs) using native mass spectrometry (MS) techniques and molecular simulations. Her work resulted in the discovery of a kinetically regulated peptide ionization mechanism that preserves the conformations during the ionization process and under native conditions, a key enabling step to further our understanding of IDPs.
Sam then pursued a second Ph.D. in Molecular Biophysics at Johns Hopkins University, giving her a unique opportunity to characterize epigenetic regulatory pathways associated with chromatin accessibility and organization. More specifically, she developed a novel technique to identify DNA-protein interactions at base-pair resolution. Using this technique, she identified functional mechanisms of general regulatory factors (GRFs) in establishing nucleosome-depleted regions on genomic DNA and regulating the transcription of housekeeping genes. Her work revealed a kinetic competition between GRFs and core histones that determines nucleosome assembly and repositioning. This study provides significant insight into the potential (mis)function of GRF mutants associated with cancer and developmental disorders.
Sam went on to establish her independent lab at Washington University as a Cori Fellow and secured generous funding to characterize the neuroepigenetics of mental and developmental disorders, including Rahman syndrome (RMNS), a poorly understood orphan disease caused by frameshift mutations in an essential linker histone. Sam proposed a consolidative approach to characterize these variants using native MS, proteomics, and single-molecule approaches. She also developed a novel technique to determine the genome-wide distribution of linker histones and their impact on epigenetic modifications and chromatin conformation. This provides new therapeutic opportunities to alleviate RMNS symptoms, prevent its progression into adulthood, and eliminate its potential emergence in offspring.
Currently, Sam is a scientist on the platform team at General Proximity, investigating the structure and conformation of intrinsically disordered proteins and their interactions with potential target drugs. When not immersed in her research, she enjoys swimming, long walks in nature, and spending time with her beloved cats.
