Journey of Poly-Nucleotides through OmpF Porin

2015 ◽  
Vol 119 (20) ◽  
pp. 6113-6128
Author(s):  
Hamid Hadi-Alijanvand ◽  
Maryam Rouhani
Keyword(s):  
Ompf Porin

Mutations that alter the pore function of the ompF porin of Escherichia coli K12

1988 ◽  
Vol 203 (4) ◽  
pp. 961-970 ◽  
Author(s):  
S.A. Benson ◽  
J.L.L. Occi ◽  
B.A. Sampson
Keyword(s):  
Escherichia Coli ◽  
Ompf Porin ◽  
Escherichia Coli K12

Linearity, saturation and blocking in a large multiionic channel: Divalent cation modulation of the OmpF porin conductance

2011 ◽  
Vol 404 (1) ◽  
pp. 330-334 ◽  
Author(s):  
Elena García-Giménez ◽  
M. Lidón López ◽  
Vicente M. Aguilella ◽  
Antonio Alcaraz
Keyword(s):  
Divalent Cation ◽  
Ompf Porin

scholarly journals Regulation of ompF porin expression by salicylate in Escherichia coli.

1991 ◽  
Vol 173 (18) ◽  
pp. 5631-5638 ◽  
Author(s):  
J L Rosner ◽  
T J Chai ◽  
J Foulds
Keyword(s):  
Escherichia Coli ◽  
Ompf Porin

Impedance Spectroscopy of OmpF Porin Reconstituted into a Mercury-Supported Lipid Bilayer

Langmuir ◽  
2006 ◽  
Vol 22 (3) ◽  
pp. 1341-1346 ◽  
Author(s):  
Lucia Becucci ◽  
Maria Rosa Moncelli ◽  
Rolando Guidelli
Keyword(s):  
Impedance Spectroscopy ◽  
Lipid Bilayer ◽  
Supported Lipid Bilayer ◽  
Ompf Porin

Imaging of reconstituted biological channels at molecular resolution by atomic force microscopy

1993 ◽  
Vol 265 (3) ◽  
pp. C851-C856 ◽  
Author(s):  
R. Lal ◽  
H. Kim ◽  
R. M. Garavito ◽  
M. F. Arnsdorf
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Internal Control ◽  
Imaging Method ◽  
Buffer Solution ◽  
Electron Microscopic ◽  
Ompf Porin ◽  
Force Microscopy ◽  
Atomic Force ◽  
Rectangular Pattern

Using atomic force microscopy (AFM), we obtained high-resolution surface images of the bacterial outer membrane channels Escherichia coli OmpF porin and Bordetella pertussis porin that were reconstituted in artificial bilayer membranes as two-dimensional crystalline arrays. These porins were chosen because they are among the most extensively studied proteins of this type and are known for their well-defined crystalline nature in the native membrane. Such reconstituted membrane proteins are ideal specimens to assess the suitability and resolution of AFM for imaging biomembranes and associated proteins. Although OmpF porin often showed a mixed pattern of rectangular and hexagonal arrays with approximately 8.4 x 9.8- and approximately 7.2-nm-spacings, respectively, B. pertussis porin showed mostly a rectangular pattern with an approximately 7.9 x 13.8-nm spacing. The packing patterns of the E. coli OmpF porin in the membrane are very close to those found in electron-microscopic studies. When B. pertussis porin was imaged in a buffer solution, its trimeric subunits were apparently resolved, and the surface of each monomer revealed beadlike structures. This is the first report of such a high-resolution structural analysis of B. pertussis porin by any imaging method. We also imaged the lipid bilayer itself as an internal control for imaging and to further ascertain the resolution. Individual polar head groups of bilayer lipid molecules were resolved, suggesting the intrinsic resolution of AFM for bioimaging.

scholarly journals Static light scattering studies of OmpF porin: Implications for integral membrane protein crystallization

2000 ◽  
Vol 9 (8) ◽  
pp. 1559-1566 ◽  
Author(s):  
Carl Hitscherich ◽  
Margaret Allaman ◽  
John Wiencek ◽  
Jeffrey Kaplan ◽  
Patrick J. Loll
Keyword(s):  
Light Scattering ◽  
Membrane Protein ◽  
Protein Crystallization ◽  
Integral Membrane Protein ◽  
Static Light Scattering ◽  
Ompf Porin ◽  
Membrane Protein Crystallization

Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy

Science ◽  
1995 ◽  
Vol 268 (5207) ◽  
pp. 92-94 ◽  
Author(s):  
F. Schabert ◽  
C Henn ◽  
A Engel
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
Ompf Porin ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Permeation Pathways of Cations and Anions in the OmpF Porin Channel using Anomalous X-Ray Scattering

2013 ◽  
Vol 104 (2) ◽  
pp. 183a
Author(s):  
Balasundaresan Dhakshnamoorthy ◽  
Lydia Blachowicz ◽  
Benoit Roux
Keyword(s):  
Ompf Porin ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Molecular basis for the polyamine-OmpF porin interactions: inhibitor and mutant studies 1 1Edited by G. von Heijne

2000 ◽  
Vol 297 (4) ◽  
pp. 933-945 ◽  
Author(s):  
Ramkumar Iyer ◽  
Zhiqian Wu ◽  
Patrick M Woster ◽  
Anne H Delcour
Keyword(s):  
Molecular Basis ◽  
Ompf Porin

Molecular origin of the cation selectivity in OmpF porin: single channel conductances vs. free energy calculation

2003 ◽  
Vol 104 (3) ◽  
pp. 591-603 ◽  
Author(s):  
Christophe Danelon ◽  
Atsushi Suenaga ◽  
Mathias Winterhalter ◽  
Ichiro Yamato
Keyword(s):  
Free Energy ◽  
Single Channel ◽  
Free Energy Calculation ◽  
Energy Calculation ◽  
Ompf Porin ◽  
Cation Selectivity ◽  
Molecular Origin
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