Elizabeth P. Carpenter (original) (raw)

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British biologist

Elizabeth P. Carpenter is a British structural biologist who is a professor at the Nuffield Department of Medicine in Oxford. She solved the three-dimensional structure of human membrane proteins using X-ray crystallography. Carpenter uses X-ray crystallography to understand the atomic positions within proteins.

Early life and education

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Carpenter studied biochemistry at the University of Cambridge. She moved to Birkbeck, University of London for doctoral research, where she studied biochemistry and crystallography.[1] After completing her doctorate, Carpenter moved to the National Institute for Health Research, which was based at Imperial College London and solved the structures of proteins involved in DNA repair.[1] She also investigated toxoplasmosis and muste movement.[1]

Research and career

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Carpenter is interested in understanding the structure and function of proteins. She studies proteins embedded within cell membranes.[1] The proteins are large hydrophobic surfaces, and understanding their structure is an important step in unravelling the processes of molecules and signals across cell membranes.[1][2] She established the Membrane Protein Laboratory at the Diamond Light Source in 2007.[1][3] In 2009, she moved to the Structural Genomics Consortium at the University of Oxford.[1]

Carpenter was the first to describe the structure of the human ABC-transporter ABC10. ABC10 is a mitrochonridal protein that is important in the production of heme. She has studied premature ageing syndromes that are caused by failure of the lamin proteins, and the role of the metalloprotease ZMPSTE24.[4] She has also studied human ion channels, including TREK-2, a K2P protein that gives rise to the background leak current that contributes to membrane potential.[4]

Selected publications

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• Elisabeth P Carpenter; Konstantinos Beis; Alexander Cameron; So Iwata (11 August 2008). "Overcoming the challenges of membrane protein crystallography". Current Opinion in Structural Biology. 18 (5): 581–586. doi:10.1016/J.SBI.2008.07.001. ISSN 0959-440X. PMC 2580798. PMID 18674618. Wikidata Q34803434.
• Simone Weyand; Tatsuro Shimamura; Shunsuke Yajima; et al. (16 October 2008). "Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter". Science. 322 (5902): 709–713. Bibcode:2008Sci...322..709W. doi:10.1126/SCIENCE.1164440. ISSN 0036-8075. PMC 2885439. PMID 18927357. Wikidata Q27652531.
• Simon Newstead; David Drew; Alexander Cameron; et al. (3 December 2010). "Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2". The EMBO Journal. 30 (2): 417–426. doi:10.1038/EMBOJ.2010.309. ISSN 0261-4189. PMC 3025455. PMID 21131908. Wikidata Q27666182.

1. ^ a b c d e f g "Carpenter". SGC. 2019-04-25. Retrieved 2021-09-17.
2. ^ "Liz Carpenter". www.medsci.ox.ac.uk. Retrieved 2021-09-17.
3. ^ "New UK laboratory to focus on important medical targets - - Diamond Light Source". www.diamond.ac.uk. Retrieved 2021-09-17.
4. ^ a b "Liz Carpenter". www.ndm.ox.ac.uk. Retrieved 2021-09-17.