Characterization of the motion of membrane proteins using high-speed atomic force microscopy (Q57012648)

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7 February 2020

title

Characterization of the motion of membrane proteins using high-speed atomic force microscopy (English)

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7 February 2020

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7 February 2020

Perrine Paul-Gilloteaux

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7 February 2020

Mohamed Husain

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7 February 2020

Henning Stahlberg

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7 February 2020

James Sturgis

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7 February 2020

Simon Scheuring

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7 February 2020

author name string

Jonathan Khao

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7 February 2020

Mohamed Chami

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7 February 2020

Jean-Pierre Duneau

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publication date

8 July 2012

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7 February 2020

published in

Nature Nanotechnology

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volume

7

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issue

8

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page(s)

525-529

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Membranes are more mosaic than fluid

7 February 2020

cites work

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Porin channel triplets merge into single outlets in Escherichia coli outer membranes.

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Software for drift compensation, particle tracking and particle analysis of high-speed atomic force microscopy image series

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Crystal structures explain functional properties of two E. coli porins

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High-speed atomic force microscopy reveals rotary catalysis of rotorless F₁-ATPase.

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Proteins of the outer membrane of gram-negative bacteria

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Kinetics of bimolecular reactions in model bilayers and biological membranes. A critical review.

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Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding

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PubMed

https://pubmed.ncbi.nlm.nih.gov/22772862

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

New major outer membrane proteins found in an Escherichia coli tolF mutant resistant to bacteriophage TuIb

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22772862

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NNANO.2012.109

1 reference

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7 February 2020

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