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

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

45 Zitate (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.

OriginalspracheEnglisch
Seiten (von - bis)759-763
Seitenumfang5
FachzeitschriftNano Letters
Jahrgang15
Ausgabenummer1
DOIs
PublikationsstatusVeröffentlicht - 14 Jän. 2015

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