High-speed AFM images of thermal motion provide stiffness map of interfacial membrane protein moieties.
Nano Lett
; 15(1): 759-63, 2015 Jan 14.
Article
em En
| MEDLINE
| ID: mdl-25516527
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.
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01-internacional
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MEDLINE
Idioma:
En
Ano de publicação:
2015
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Article