Literature DB >> 19322865

On the function and structure of synthetically modified porins.

Simon Reitz1, Menekse Cebi, Philipp Reiss, Gregor Studnik, Uwe Linne, Ulrich Koert, Lars-Oliver Essen.   

Abstract

The attachment of modulators to a trimeric porin ion channel was investigated (see picture of the trimer with a crown ether modulator (orange)). The interplay of modulator and protein is essential for the conformational heterogeneity of the hybrid channel. Single-site attachment in large pores is not sufficient to change the electrophysiological characteristics of the pores-such change requires additional noncovalent interactions or second-site attachments.

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Year:  2009        PMID: 19322865     DOI: 10.1002/anie.200900457

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


  3 in total

1.  Structures of the OmpF porin crystallized in the presence of foscholine-12.

Authors:  Georgia Kefala; Chihoon Ahn; Martin Krupa; Luis Esquivies; Innokentiy Maslennikov; Witek Kwiatkowski; Senyon Choe
Journal:  Protein Sci       Date:  2010-05       Impact factor: 6.725

2.  The binding of antibiotics in OmpF porin.

Authors:  Brigitte K Ziervogel; Benoît Roux
Journal:  Structure       Date:  2012-11-29       Impact factor: 5.006

3.  Divalent Metal Ion Transport across Large Biological Ion Channels and Their Effect on Conductance and Selectivity.

Authors:  Elena García-Giménez; Antonio Alcaraz; Vicente M Aguilella
Journal:  Biochem Res Int       Date:  2012-09-13
  3 in total

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