Joan-Emma Shea
Born1972 (age 5152)
Alma materMcGill University
Massachusetts Institute of Technology
Scientific career
InstitutionsUniversity of California, San Diego
ThesisBrownian motion in a non-equilibrium bath (1997)

Joan-Emma Shea is an American chemist who is a professor at the University of California, Santa Barbara. Her research applies statistical and computational approaches to address biological problems. She is a Fellow of both the American Physical Society and the American Chemical Society, and the editor-in-chief of the Journal of Physical Chemistry.

Early life and education

Shea was born in Santa Barbara, California.[1] She was an undergraduate student at McGill University and a doctoral student at the Massachusetts Institute of Technology, where her research considered Brownian motion.[2] She was awarded a National Sciences and Engineering Research Council of Canada fellowship, and joined Charles L. Brooks III at the University of California, San Diego and Scripps Research.[1]

Research and career

Shea joined the James Franck Institute at the University of Chicago in 2000, where she spent one year before joining the University of California, Santa Barbara.[3][4] She became a professor at the University of California, Santa Barbara in 2008. Her work considers the chemistry of cellular processes, including in vivo protein folding.[5] In particular, She studies intrinsically disordered proteins, biomolecules which do not fold to a single, 3D shape, but instead rapidly interconvert between many conformations in their monomeric forms. Some intrinsically disordered proteins can self-assemble into fibrillar aggregates and/or undergo a process called liquid-liquid phase separation. Shea studies these processes using computational and statistical approaches[6]

In 2019, Shea was elected as editor-in-chief of the Journal of Physical Chemistry (A, B and C). She was the first woman to hold this position in the 124-year history of the journal.[7]

Awards and honors

Selected publications

  • Summer L Bernstein; Nicholas F Dupuis; Noel D Lazo; et al. (1 July 2009). "Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease". Nature Chemistry. 1 (4): 326–331. doi:10.1038/NCHEM.247. ISSN 1755-4330. PMC 2918915. PMID 20703363. Wikidata Q34055098.
  • Shea JE; Brooks CL 3rd (1 January 2001). "From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding". Annual Review of Physical Chemistry. 52: 499–535. doi:10.1146/ANNUREV.PHYSCHEM.52.1.499. ISSN 0066-426X. PMID 11326073. Wikidata Q30168219.{{cite journal}}: CS1 maint: numeric names: authors list (link)
  • Andriy Baumketner; Summer L Bernstein; Thomas Wyttenbach; Gal Bitan; David B Teplow; Michael T Bowers; Joan-Emma Shea (1 March 2006). "Amyloid beta-protein monomer structure: a computational and experimental study". Protein Science. 15 (3): 420–428. doi:10.1110/PS.051762406. ISSN 0961-8368. PMC 2249763. PMID 16501222. Wikidata Q42150321.

References

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