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10.1021/la500560w

http://scihub22266oqcxt.onion/10.1021/la500560w
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C4007984!4007984!24697545
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suck abstract from ncbi


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pmid24697545      Langmuir 2014 ; 30 (16): 4784-96
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  • Direct Evidence of Conformational Changes Associated with Voltage Gating in a Voltage Sensor Protein by Time-Resolved X-ray/Neutron Interferometry #MMPMID24697545
  • Tronin A; Nordgren CE; Strzalka JW; Kuzmenko I; Worcester DL; Lauter V; Freites JA; Tobias DJ; Blasie JK
  • Langmuir 2014[Apr]; 30 (16): 4784-96 PMID24697545show ga
  • The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na+, K+) channels central to neurological signal transmission can function as a distinct module. When linked to an otherwise voltage-insensitive, ion-selective membrane pore, the VSD imparts voltage sensitivity to the channel. Proteins homologous with the VSD have recently been found to function themselves as voltage-gated proton channels or to impart voltage sensitivity to enzymes. Determining the conformational changes associated with voltage gating in the VSD itself in the absence of a pore domain thereby gains importance. We report the direct measurement of changes in the scattering-length density (SLD) profile of the VSD protein, vectorially oriented within a reconstituted phospholipid bilayer membrane, as a function of the transmembrane electric potential by time-resolved X-ray and neutron interferometry. The changes in the experimental SLD profiles for both polarizing and depolarizing potentials with respect to zero potential were found to extend over the entire length of the isolated VSD?s profile structure. The characteristics of the changes observed were in qualitative agreement with molecular dynamics simulations of a related membrane system, suggesting an initial interpretation of these changes in terms of the VSD?s atomic-level 3-D structure.
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