2 research outputs found
Hydrophobic Effects on Tyrosyl Ring 1H Chemical Shifts in Peptides
Get PDFposter abstractHydrophobic environmental effects on tyrosine are measurable by 1H NMR spectroscopy
and can allow us to detect interactions between peptides and lipid membranes. We first
investigated the effects of hydrophobic environments on the 1H chemical shifts of
tyrosine ring protons by using varying concentrations of isopropanol to mimic and
calibrate the effects of hydrophobicity. Compared with this calibration, we then measured
the interaction of tyrosine-containing peptides with sonicated unilamellar vesicles of
phosholipids such as phosphatidylcholine and phosphatidylserine that are commonly
found in biological membranes
Hydrophobic Effects on Tyrosyl Ring 1H Chemical Shifts in Peptides
No full textposter abstractHydrophobic environmental effects on tyrosine are measurable by 1H NMR spectroscopy
and can allow us to detect interactions between peptides and lipid membranes. We first
investigated the effects of hydrophobic environments on the 1H chemical shifts of
tyrosine ring protons by using varying concentrations of isopropanol to mimic and
calibrate the effects of hydrophobicity. Compared with this calibration, we then measured
the interaction of tyrosine-containing peptides with sonicated unilamellar vesicles of
phosholipids such as phosphatidylcholine and phosphatidylserine that are commonly
found in biological membranes
