Hydrophobic Effects on Tyrosyl Ring 1H Chemical Shifts in Peptides

Simple item page
dc.contributor.authorLiantu, Rosy S.
dc.contributor.authorRay, Bruce D.
dc.contributor.authorPetrache, Horia I.
dc.date.accessioned2016-07-11T18:05:09Z
dc.date.available2016-07-11T18:05:09Z
dc.date.issued2016-04-08
dc.descriptionposter abstracten_US
dc.description.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.en_US
dc.identifier.citationRosy S. Liantu, Bruce D. Ray, and Horia I. Petrache. 2016, April 8. Hydrophobic Effects on Tyrosyl Ring 1H Chemical Shifts in Peptides. Poster session presented at IUPUI Research Day 2016, Indianapolis, Indiana.en_US
dc.identifier.urihttps://hdl.handle.net/1805/10349
dc.language.isoen_USen_US
dc.publisherOffice of the Vice Chancellor for Researchen_US
dc.subjectHydrophobic Effectsen_US
dc.subjectenvironmental effectsen_US
dc.subjecttyrosineen_US
dc.subject1H NMR spectroscopyen_US
dc.titleHydrophobic Effects on Tyrosyl Ring 1H Chemical Shifts in Peptidesen_US
dc.typePosteren_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Liantu.pdf
Size:
6.72 KB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.88 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
IUPUI Research Day 2016