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For many years, Dr. Fleming studied the energetics of transmembrane helix-helix interactions. She developed theory to describe their association reactions, defined conditions for “forced cohabitation” of helices in micelles; and discovered thermodynamic coupling in transmembrane helix-helix dimerization. Recently, Dr. Fleming’s laboratory has turned their focus to the water-to-bilayer protein-folding problem. Using transmembrane beta-barrels, her group quadrupled the number of known membrane protein stabilities; developed a novel side chain hydrophobicity scale; and experimentally demonstrated that transfer free energies of aromatic side chains follow the polarity gradient inherent in the structure of a phospholipid bilayer. In addition to experiments, Dr. Fleming’s group uses molecular simulations to address questions of membrane protein structure in phospholipid bilayers and has applied ODE methods to develop a quantitative flux model that describes the sorting of membrane proteins in the periplasms of bacterial envelopes. Coupled with experiments, this holistic approach identifies functions of chaperones and has defined the role played by the essential BAM complex.
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Lin Shen,Karen G. Fleming
Biophysical journalno. 3 (2024): 301a-302a
BIOPHYSICAL JOURNALno. 16 (2024): 2379-2391
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (2023): A225-A225
European Biophysics Journalno. 4 (2023): 415-425
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERSno. SUPPL 1 (2023): S23-S23
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Proceedings of the National Academy of Sciences of the United States of Americano. 44 (2023): e2315655120-e2315655120
Taylor A. Devlin,Dagan C. Marx, Anneliese Faustino,Michaela Roskopf, Stephen D. Fried,Karen G. Fleming
wos(2022)
Proceedings of the National Academy of Sciences of the United States of Americano. 48 (2022)
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#Papers: 126
#Citation: 5050
H-Index: 41
G-Index: 70
Sociability: 5
Diversity: 3
Activity: 60
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