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- W2023922054 abstract "Proteins may undergo multiple conformational changes required for their function. One strategy used to estimate target-site positions in unknown structural conformations involves single-pair resonance energy transfer (RET) distance measurements. However, interpretation of inter-residue distances is difficult when applied to three-dimensional structural rearrangements, especially in homomeric systems. We developed a positioning method using inverse trilateration/triangulation to map target sites within a homomeric protein in all defined states, with simultaneous functional recordings. The procedure accounts for probe diffusion to accurately determine the three-dimensional position and confidence region of lanthanide LRET donors attached to a target site (one per subunit), relative to a single fluorescent acceptor placed in a static site. As first application, the method is used to determine the position of a functional voltage-gated potassium channel's voltage sensor. Our results verify the crystal structure relaxed conformation and report on the resting and active conformations for which crystal structures are not available." @default.
- W2023922054 created "2016-06-24" @default.
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- W2023922054 date "2012-10-01" @default.
- W2023922054 modified "2023-10-16" @default.
- W2023922054 title "Nano-Positioning System for Structural Analysis of Functional Homomeric Proteins in Multiple Conformations" @default.
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- W2023922054 doi "https://doi.org/10.1016/j.str.2012.08.022" @default.
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