1930
DOI: 10.1007/bf01861219
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Über die Komplexbildung zwischen Coffein und Salizylsäure

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Cited by 8 publications
(1 citation statement)
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“…The X-ray structural studies clarified the orientation of hydrocarbon chains . The hydrophobic effect, attributed to entropy-driven changes in water structure, which was initially studied in connection with colloid behavior, waterproofing of textiles, and protein folding, , was recognized as the driving force in the formation of the bilayer . The structure of the phospholipid bilayer in the gel phase was studied by neutron diffraction. The headgroup dipoles change orientations in response to the overall charge of the bilayer .…”
Section: Individual Steps Vs Propertiesmentioning
confidence: 99%
“…The X-ray structural studies clarified the orientation of hydrocarbon chains . The hydrophobic effect, attributed to entropy-driven changes in water structure, which was initially studied in connection with colloid behavior, waterproofing of textiles, and protein folding, , was recognized as the driving force in the formation of the bilayer . The structure of the phospholipid bilayer in the gel phase was studied by neutron diffraction. The headgroup dipoles change orientations in response to the overall charge of the bilayer .…”
Section: Individual Steps Vs Propertiesmentioning
confidence: 99%