Source data for paper "Voltage Sensor Conformations Induced by LQTS-associated Mutations in hERG Potassium Channels"
<p dir="ltr">In this study, we employed a combination of techniques including nonsense suppression-mediated incorporation of noncanonical amino acids for site-specific fluorescence labeling, FLIM-based transition metal Förster resonance energy transfer (FLIM-tmFRET), and MD simulatio...
محفوظ في:
| المؤلف الرئيسي: | |
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| مؤلفون آخرون: | , , , , |
| منشور في: |
2025
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| الموضوعات: | |
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| الملخص: | <p dir="ltr">In this study, we employed a combination of techniques including nonsense suppression-mediated incorporation of noncanonical amino acids for site-specific fluorescence labeling, FLIM-based transition metal Förster resonance energy transfer (FLIM-tmFRET), and MD simulations to examine the impact of a LQTS-associated mutation on conformational rearrangements of hERG voltage sensors in transfected cell lines. We applied a dual stop-codon suppression strategy relying on a small fluorescent noncanonical amino acid to discern and dissect the conformational heterogeneity of voltage sensors by analyzing the frequency-domain phasor plot function of FLIM-tmFRET. This methodology has significant potential for broad applications, offering an effective approach to quantitatively assess the movement, states, dynamics, and energetics of voltage sensors in ion channels.</p> |
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