ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
Imaging the Electrostatic Potential of Transmembrane Channels: Atomic Probe Microscopy of OmpF Porin
dc.contributor.author | Philippsen, Ansgar | |
dc.contributor.author | Engel, Andreas | |
dc.contributor.author | Schirmer, Tilman | |
dc.contributor.author | Roux, Benoît | |
dc.contributor.author | Müller, Daniel J. | |
dc.contributor.author | Im, Wonpil | |
dc.date.accessioned | 2015-04-17T20:06:16Z | |
dc.date.available | 2015-04-17T20:06:16Z | |
dc.date.issued | 2002-03 | |
dc.identifier.citation | Philippsen, Ansgar, Wonpil Im, Andreas Engel, Tilman Schirmer, Benoit Roux, and Daniel J. Müller. "Imaging the Electrostatic Potential of Transmembrane Channels: Atomic Probe Microscopy of OmpF Porin." Biophysical Journal 82.3 (2002): 1667-676. http://dx.doi.org/10.1016/S0006-3495(02)75517-3. | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/17440 | |
dc.description | This is the published version. Copyright 2002 by Elsevier. | en_US |
dc.description.abstract | The atomic force microscope (AFM) was used to image native OmpF porin and to detect the electrostatic potential generated by the protein. To this end the OmpF porin trimers from Escherichia coli was reproducibly imaged at a lateral resolution of ∼0.5 nm and a vertical resolution of ∼0.1 nm at variable electrolyte concentrations of the buffer solution. At low electrolyte concentrations the charged AFM probe not only contoured structural details of the membrane protein surface but also interacted with local electrostatic potentials. Differences measured between topographs recorded at variable ionic strength allowed mapping of the electrostatic potential of OmpF porin. The potential map acquired by AFM showed qualitative agreement with continuum electrostatic calculations based on the atomic OmpF porin embedded in a lipid bilayer at the same electrolyte concentrations. Numerical simulations of the experimental conditions showed the measurements to be reproduced quantitatively when the AFM probe was included in the calculations. This method opens a novel avenue to determine the electrostatic potential of native protein surfaces at a lateral resolution better than 1 nm and a vertical resolution of ∼0.1 nm. | en_US |
dc.publisher | Elsevier | en_US |
dc.title | Imaging the Electrostatic Potential of Transmembrane Channels: Atomic Probe Microscopy of OmpF Porin | en_US |
dc.type | Article | |
kusw.kuauthor | Im, Wonpil | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1016/S0006-3495(02)75517-3 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item does not meet KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |