Folding of a monomeric porin, OmpG, in detergent solution (Q30164583)

9 June 2017

title

Folding of a monomeric porin, OmpG, in detergent solution (English)

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9 June 2017

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Hagan Bayley

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language of work or name

English

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publication date

1 August 2003

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9 June 2017

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9 June 2017

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9 June 2017

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9 June 2017

page(s)

9453-9465

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A novel mutation, cog, which results in production of a new porin protein (OmpG) of Escherichia coli K-12.

9 June 2017

cites work

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Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy

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Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness

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Membrane Assembly of Circularly Permuted Variants of theE. coliOuter Membrane Protein OmpA

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Lock On/Off Disulfides Identify the Transmembrane Signaling Helix of the Aspartate Receptor

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General and specific porins from bacterial outer membranes

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The assembly pathway of outer membrane protein PhoE of Escherichia coli

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Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli

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Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein

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Characterisation of the porin of Rhodobacter capsulatus 37b4 in planar lipid bilayers.

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Kinetics of folding and membrane insertion of a beta-barrel membrane protein.

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Methods to estimate the conformation of proteins and polypeptides from circular dichroism data

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Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide

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The orientation of porin OmpF in the outer membrane of Escherichia coli.

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Projection structure of the monomeric porin OmpG at 6 A resolution.

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https://opencitations.net/index/coci/api/v1/references/10.1021/BI0344228

Identifiers

DOI

10.1021/BI0344228

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9 June 2017

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