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Barbara Imperiali on Muck Rack

Barbara Imperiali

As seen in: Wiley Online Library, PLOS ONE, Royal Society of Chemistry, BioRxiv, Cell Press, The Journal of Biological Chemistry
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Articles

Correlating membrane‐protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single‐molecule FRET

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By Hugh Higinbotham, Christine A Arbour, Barbara Imperiali
| Wiley Online Library Verified
1 INTRODUCTION Integral membrane proteins (IMPs) comprise approximately 25% of proteomes across kingdoms of life (Krogh et al., 2001). The specific composition and physicochemical properties of membranes vary widely, and the diverse interplay of this environment with IMP structure and function is a rich target for investigation (Brown et al., 2025; Levental & Lyman, 2023; Teo et al., 2019).
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Selection of nanobodies against liponanoparticle‐embedded membrane proteins by yeast‐surface display

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By Greg J. Dodge, Hayley L Knox, Brian Cho, Barbara Imperiali
| Wiley Online Library Verified
Supporting Information Filename Description pro70293-sup-0001-Supinfo.docxWord 2007 document , 4.5 MB Table S1. Primers used for Nbs. Figure S1. SDS-PAGE showing purification of enzymes in various polymers with their predicted molecular weight listed. Black arrow points at the band of interest. Figure S2. Assessment of selected WbaP yeast population specificity. Each selected yeast population from the naïve library to population 0.3 was assessed by analytical flow cytometry for binding to A.
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Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET

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By Hugh Higinbotham, Christine A Arbour, Barbara Imperiali
| BioRxiv
Abstract We present a strategy that deploys structural bioinformatics, molecular simulation, and single-molecule FRET microscopy for observing the ligand-dependent conformational dynamics of integral membrane proteins in situ.
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