3 research outputs found
High-Speed AFM Images of Thermal Motion Provide Stiffness Map of Interfacial Membrane Protein Moieties
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
High-Speed AFM Images of Thermal Motion Provide Stiffness Map of Interfacial Membrane Protein Moieties
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
High-Speed AFM Images of Thermal Motion Provide Stiffness Map of Interfacial Membrane Protein Moieties
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