2019
DOI: 10.1016/j.cplett.2019.04.086
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Tuning the conformations of hemoglobin via interactions with single-chain and Gemini quaternary ammonium surfactants

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“…Luo et al focused on the investigations of the interactions between single-chain or gemini quaternary ammonium surfactants with hemoglobin.They observed that the interactions between the surfactants and hemoglobin were mainly caused by both electrostatic and hydrophobic interactions, and the hydrophobic chain length and linking group length of the surfactants had a significant influence on tuning the conformations of hemoglobin [130]. For their part, Amiri et al reported the interactions of gemini surfactants with ribonuclease Sa, and the results indicated that the tune of protein conformations is changed with the structure of surfactants and proteins [131].…”
Section: Applicationsmentioning
confidence: 99%
“…Luo et al focused on the investigations of the interactions between single-chain or gemini quaternary ammonium surfactants with hemoglobin.They observed that the interactions between the surfactants and hemoglobin were mainly caused by both electrostatic and hydrophobic interactions, and the hydrophobic chain length and linking group length of the surfactants had a significant influence on tuning the conformations of hemoglobin [130]. For their part, Amiri et al reported the interactions of gemini surfactants with ribonuclease Sa, and the results indicated that the tune of protein conformations is changed with the structure of surfactants and proteins [131].…”
Section: Applicationsmentioning
confidence: 99%