High-speed AFM images of thermal motion provide stiffness map of interfacial membrane protein moieties

Johannes Preiner, Andreas Horner, Andreas Karner, Nicole Ollinger, Christine Siligan, Peter Pohl, Peter Hinterdorfer

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

The flexibilities of extracellular loops determine ligand binding and activation of membrane receptors. Arising from fluctuations in inter- and intraproteinaceous interactions, flexibility manifests in thermal motion. Here we demonstrate that quantitative flexibility values can be extracted from directly imaging the thermal motion of membrane protein moieties using high-speed atomic force microscopy (HS-AFM). Stiffness maps of the main periplasmic loops of single reconstituted water channels (AqpZ, GlpF) revealed the spatial and temporal organization of loop-stabilizing intraproteinaceous H-bonds and salt bridges.

Original languageEnglish
Pages (from-to)759-763
Number of pages5
JournalNano Letters
Volume15
Issue number1
DOIs
Publication statusPublished - 14 Jan 2015

Keywords

  • AqpZ
  • flexibility
  • GlpF
  • high speed atomic force microscopy
  • membrane proteins
  • Single molecule
  • Aquaporins/chemistry
  • Protein Structure, Secondary
  • Escherichia coli Proteins/chemistry
  • Microscopy, Atomic Force/methods
  • Escherichia coli/chemistry

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