On the function and structure of synthetically modified porins

Angew Chem Int Ed Engl. 2009;48(26):4853-7. doi: 10.1002/anie.200900457.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crown Ethers / chemistry
  • Crystallography, X-Ray
  • Ion Channels / chemistry
  • Porins / chemistry*
  • Protein Conformation

Substances

  • Crown Ethers
  • Ion Channels
  • OmpF protein
  • Porins