期刊
NANO LETTERS
卷 15, 期 1, 页码 759-763出版社
AMER CHEMICAL SOC
DOI: 10.1021/nl504478f
关键词
Single molecule; flexibility; high speed atomic force microscopy; AqpZ; GlpF; membrane proteins
类别
资金
- European Fund for Regional Development (EFRE) [Regio 13]
- Federal State of Upper Austria
- Austrian Science Foundation (FWF) [P23466, P25844]
- Austrian Science Fund (FWF) [P 23466, P 25844] Funding Source: researchfish
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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